Gria1 encodes GluA1 (GluR1, GluR-A), a pore-forming subunit of AMPA-type ionotropic glutamate receptors. GluA1 assembles with GluA2 (most commonly), GluA3 or GluA4, or as homomers, into tetrameric glutamate-gated cation channels together with auxiliary TARP and cornichon subunits; GluA1/GluA2 receptors with TARP gamma-8 are the principal AMPA receptors at hippocampal synapses, where they mediate fast excitatory transmission from the postsynaptic density membrane of dendritic spines. GluA1 is not edited at the pore Q/R site, so GluA1 homomers and other GluA2-lacking receptors are Ca2+-permeable and inwardly rectifying. Flip/flop splicing tunes desensitization. The cytoplasmic C-terminal tail carries a type I PDZ ligand that binds SAP97 and phosphorylation sites (Ser831 for CaMKII/PKC, Ser845 for PKA in mature numbering) plus a Loop1 CaMKII site, palmitoylation and ubiquitination sites that control surface delivery, synaptic insertion and endocytosis. Activity-dependent insertion of GluA1-containing receptors into synapses is a principal expression mechanism of long-term potentiation, and their removal contributes to long-term depression; GluA1 trafficking is also remodelled in drug-, stress- and learning-related plasticity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001540 amyloid-beta binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Amyloid-beta binding; soluble Abeta oligomers (ADDLs) bind spines expressing surface AMPA receptor complexes, preferentially GluA2-containing ones. Reason: Co-immunoprecipitation and photo-crosslinking show that ADDLs associate with AMPA receptor complexes on dendritic spines (PMID:20032460). This is a pathological ligand interaction of the receptor complex (with a GluA2 preference), not part of the physiological function of GluA1, so it is kept as non-core. Supporting Evidence: PMID:20032460 we found that ADDLs interact preferentially with GluR2-containing complexes PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors |
| GO:0001540 amyloid-beta binding | IPI PMID:20032460 Inhibition of calcineurin-mediated endocytosis and alpha-ami... | KEEP AS NON CORE | Summary: Amyloid-beta binding; soluble Abeta oligomers (ADDLs) bind spines expressing surface AMPA receptor complexes, preferentially GluA2-containing ones. Reason: Co-immunoprecipitation and photo-crosslinking show that ADDLs associate with AMPA receptor complexes on dendritic spines (PMID:20032460). This is a pathological ligand interaction of the receptor complex (with a GluA2 preference), not part of the physiological function of GluA1, so it is kept as non-core. Supporting Evidence: PMID:20032460 we found that ADDLs interact preferentially with GluR2-containing complexes PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors |
| GO:0001666 response to hypoxia | IEP PMID:29112674 Interleukin-10 and PD150606 modulate expression of AMPA rece... | MARK AS OVER ANNOTATED | Summary: Response to hypoxia (IEP): GluA1 protein and pSer831-GluA1 levels fall in hippocampal slices exposed to brief hypoxic episodes. Reason: An expression change of GluA1 under hypoxia is a readout of the slice state; it does not show that GluA1 executes a hypoxia response process. IEP expression data are not sufficient for a process annotation here. Supporting Evidence: PMID:29112674 ameliorate hypoxia-induced decrease in the expression of GluA1 and pSer831-GluA1 |
| GO:0001919 regulation of receptor recycling | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Regulation of receptor recycling, based on subunit-specific rules of AMPA receptor delivery to synapses. Reason: GluA1 is the recycling cargo. Its C-terminal motifs recruit PDZ proteins, which (with the trafficking machinery) do the regulating; the GluA1 tail being needed for its own trafficking does not make GluA1 a regulator of receptor recycling as a process. The trafficking role is captured by PDZ domain binding. Supporting Evidence: PMID:11348590 GluR1/GluR2 receptors are added to synapses during plasticity; this requires interactions between GluR1 and group I PDZ domain proteins. |
| GO:0001919 regulation of receptor recycling | IMP PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | MARK AS OVER ANNOTATED | Summary: Regulation of receptor recycling, based on subunit-specific rules of AMPA receptor delivery to synapses. Reason: GluA1 is the recycling cargo. Its C-terminal motifs recruit PDZ proteins, which (with the trafficking machinery) do the regulating; the GluA1 tail being needed for its own trafficking does not make GluA1 a regulator of receptor recycling as a process. The trafficking role is captured by PDZ domain binding. Supporting Evidence: PMID:11348590 GluR1/GluR2 receptors are added to synapses during plasticity; this requires interactions between GluR1 and group I PDZ domain proteins. |
| GO:0001965 G-protein alpha-subunit binding | IPI PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | MARK AS OVER ANNOTATED | Summary: G-protein alpha-subunit binding (IPI, with Gnas), from the beta2AR-Gs-adenylyl cyclase-PKA-GluA1 signalling complex. Reason: The cited study describes a supramolecular complex in which GluA1 is linked to the beta2AR through stargazin and PSD-95; co-precipitation of Galpha-s with GluA1 reflects membership of this complex, not a direct GluA1-Galpha binding activity. Full text not available; flagged rather than removed. Supporting Evidence: PMID:19942860 which is linked to the beta(2)AR through stargazin and PSD-95 and their homologues PMID:19942860 Assembly of all proteins involved in the classic beta(2)AR-cAMP cascade into a supramolecular signalling complex |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:11773314 Voltage and concentration dependence of Ca(2+) permeability ... | MODIFY | Summary: Glutamate-gated receptor activity; GluA1 forms glutamate-gated cation channels with AMPA-selective pharmacology. Reason: Correct but less specific than the evidence: recombinant GluA1 receptors show AMPA > glutamate > kainate pharmacology and AMPA-gated currents. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant of GO:0004970 that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:11773314 For GluR-A(Q) channels, P(Ca)/P(Na) derived from all three approaches was concentration independent |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:1699275 Flip and flop: a cell-specific functional switch in glutamat... | MODIFY | Summary: Glutamate-gated receptor activity; GluA1 forms glutamate-gated cation channels with AMPA-selective pharmacology. Reason: Correct but less specific than the evidence: recombinant GluA1 receptors show AMPA > glutamate > kainate pharmacology and AMPA-gated currents. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant of GO:0004970 that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:1699275 impart different pharmacological and kinetic properties on currents evoked by L-glutamate or AMPA, but not those evoked by kainate PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:1709304 Ca2+ permeability of KA-AMPA--gated glutamate receptor chann... | MODIFY | Summary: Glutamate-gated receptor activity; GluA1 forms glutamate-gated cation channels with AMPA-selective pharmacology. Reason: Correct but less specific than the evidence: recombinant GluA1 receptors show AMPA > glutamate > kainate pharmacology and AMPA-gated currents. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant of GO:0004970 that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:1709304 At physiological resting potentials, KA and AMPA elicited inward calcium currents in oocytes expressing GluR1, GluR3, and GluR1 plus GluR3. |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:17409242 Electrophysiological properties of AMPA receptors are differ... | MODIFY | Summary: Glutamate-gated receptor activity; GluA1 forms glutamate-gated cation channels with AMPA-selective pharmacology. Reason: Correct but less specific than the evidence: recombinant GluA1 receptors show AMPA > glutamate > kainate pharmacology and AMPA-gated currents. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant of GO:0004970 that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:17409242 agonist-induced currents of all homomeric AMPA receptor subunits as well as all heteromeric combinations tested are significantly potentiated when coexpressed with members of the TARP family |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:2166337 A family of AMPA-selective glutamate receptors. | MODIFY | Summary: Glutamate-gated receptor activity; GluA1 forms glutamate-gated cation channels with AMPA-selective pharmacology. Reason: Correct but less specific than the evidence: recombinant GluA1 receptors show AMPA > glutamate > kainate pharmacology and AMPA-gated currents. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant of GO:0004970 that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:2480522 Cloning by functional expression of a member of the glutamat... | MODIFY | Summary: Glutamate-gated receptor activity; GluA1 forms glutamate-gated cation channels with AMPA-selective pharmacology. Reason: Correct but less specific than the evidence: recombinant GluA1 receptors show AMPA > glutamate > kainate pharmacology and AMPA-gated currents. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant of GO:0004970 that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:2480522 The cDNA encodes a single protein of relative molecular mass (Mr) 99,800 which on expression in oocytes forms a functional ion channel PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate |
| GO:0004970 glutamate-gated receptor activity | ISO GO_REF:0000121 | MODIFY | Summary: Glutamate-gated receptor activity; GluA1 forms glutamate-gated cation channels with AMPA-selective pharmacology. Reason: Correct but less specific than the evidence: recombinant GluA1 receptors show AMPA > glutamate > kainate pharmacology and AMPA-gated currents. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant of GO:0004970 that the gene already carries by IBA and IDA. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0004971 AMPA glutamate receptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: AMPA glutamate receptor activity: GluA1 is a pore-forming subunit of AMPA-type ionotropic glutamate receptors. Reason: Core molecular function. Recombinant GluA1 forms AMPA-selective glutamate-gated cation channels; it co-assembles with GluA2, TARPs and cornichons in native AMPA receptors. Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. |
| GO:0004971 AMPA glutamate receptor activity | IDA PMID:19265014 Functional proteomics identify cornichon proteins as auxilia... | ACCEPT | Summary: AMPA glutamate receptor activity: GluA1 is a pore-forming subunit of AMPA-type ionotropic glutamate receptors. Reason: Core molecular function. Recombinant GluA1 forms AMPA-selective glutamate-gated cation channels; it co-assembles with GluA2, TARPs and cornichons in native AMPA receptors. Supporting Evidence: PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. PMID:19265014 Cornichons increase surface expression of AMPARs, and they alter channel gating by markedly slowing deactivation and desensitization kinetics. |
| GO:0004971 AMPA glutamate receptor activity | IEA GO_REF:0000120 | ACCEPT | Summary: AMPA glutamate receptor activity: GluA1 is a pore-forming subunit of AMPA-type ionotropic glutamate receptors. Reason: Core molecular function. Recombinant GluA1 forms AMPA-selective glutamate-gated cation channels; it co-assembles with GluA2, TARPs and cornichons in native AMPA receptors. Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. |
| GO:0004971 AMPA glutamate receptor activity | ISO GO_REF:0000121 | ACCEPT | Summary: AMPA glutamate receptor activity: GluA1 is a pore-forming subunit of AMPA-type ionotropic glutamate receptors. Reason: Core molecular function. Recombinant GluA1 forms AMPA-selective glutamate-gated cation channels; it co-assembles with GluA2, TARPs and cornichons in native AMPA receptors. Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. |
| GO:0004971 AMPA glutamate receptor activity | ISO GO_REF:0000121 | ACCEPT | Summary: AMPA glutamate receptor activity: GluA1 is a pore-forming subunit of AMPA-type ionotropic glutamate receptors. Reason: Core molecular function. Recombinant GluA1 forms AMPA-selective glutamate-gated cation channels; it co-assembles with GluA2, TARPs and cornichons in native AMPA receptors. Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. |
| GO:0005216 monoatomic ion channel activity | IEA GO_REF:0000002 | MODIFY | Summary: Monoatomic ion channel activity (IEA, InterPro). Reason: Correct but very general. GluA1 is a glutamate-gated cation channel of the AMPA receptor class; refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant the gene carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0005515 protein binding | IPI PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:15456832 Actin/alpha-actinin-dependent transport of AMPA receptors in... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:16108831 Identification of immunoglobulin superfamily 11 (IGSF11) as ... | REMOVE | Summary: Bare protein binding (IPI with Q5U2P2, IgSF11), citing a paper on IGSF11 as a cancer immunotherapy target. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. In addition, the cited paper (full text cached) concerns human IGSF11 expression in gastrointestinal and hepatocellular carcinomas and never mentions AMPA receptors or GluA1; the GluA1-IgSF11 interaction was reported in PMID:26595655, so the reference appears mis-keyed. Supporting Evidence: PMID:16108831 Homology searches revealed that both forms of the predicted IGSF11 proteins share similarity in amino acid sequence with CXADR and ESAM. PMID:26595655 Intriguingly, IgSF11 formed a coimmunoprecipitable complex with the GluA1 and GluA2 subunits of AMPARs, but not with the GluN1 subunit of NMDARs, in rat brains |
| GO:0005515 protein binding | IPI PMID:16338934 Involvement of myosin Vb in glutamate receptor trafficking. | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:16338934 Involvement of myosin Vb in glutamate receptor trafficking. | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:18817736 AMPA receptor subunit-specific regulation by a distinct fami... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:19208802 AMPA receptor and GEF-H1/Lfc complex regulates dendritic spi... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:19208802 AMPA receptor and GEF-H1/Lfc complex regulates dendritic spi... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:19234459 Selective regulation of long-form calcium-permeable AMPA rec... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:19805317 S-nitrosylation of stargazin regulates surface expression of... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:20395454 Binding of amyloid beta peptide to beta2 adrenergic receptor... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:20534517 A kinesin signaling complex mediates the ability of GSK-3bet... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:20805473 Functional comparison of the effects of TARPs and cornichons... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:20805473 Functional comparison of the effects of TARPs and cornichons... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:21135237 Synaptic targeting of AMPA receptors is regulated by a CaMKI... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:21317873 Subunit-selective N-terminal domain associations organize th... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:21376300 Excess of de novo deleterious mutations in genes associated ... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:24418105 Direct association of the unique C-terminal tail of transmem... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:29222408 Brain insulin resistance impairs hippocampal synaptic plasti... | REMOVE | Summary: Bare protein binding (IPI). GluA1 interacts with GluA2, TARPs (stargazin/gamma-2, gamma-5), cornichon-2, PSD-95, SAP97, myosin Vb, KLC2, CaMKII, beta2AR, GEF-H1, IgSF11 and others. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not mean the reported interaction is false. The informative content of GluA1 interactions (PDZ domain binding by the C-terminal ligand, AMPA receptor complex assembly with GluA2 and auxiliary TARP/cornichon subunits) is captured elsewhere in this review. |
| GO:0005769 early endosome | IDA PMID:11100149 Distinct molecular mechanisms and divergent endocytotic path... | KEEP AS NON CORE | Summary: Early endosome: internalized AMPA receptors enter endosomal compartments after AMPA- or insulin-induced endocytosis. Reason: GluA1-containing receptors transit early and recycling endosomes during constitutive and regulated endocytosis; a real trafficking location but not where the receptor acts. Supporting Evidence: PMID:11100149 AMPA receptors internalized in response to AMPA stimulation enter a recycling endosome system file:rat/Gria1/Gria1-uniprot.txt Colocalizes with PDLIM4 in early endosomes |
| GO:0005783 endoplasmic reticulum | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Endoplasmic reticulum (ISO from mouse Gria1). Reason: Organelle-root row checked under the ORGANELLES policy: GluA1 is a multi-pass membrane protein assembled into tetramers in the ER, and the rat entry has direct ER membrane evidence (PMID:15456832, UniProt ECO:0000269). The organelle claim holds; it is a biosynthetic location, so non-core. The sub-compartment (ER membrane) is already annotated. Supporting Evidence: PMID:21317873 the extracellular, membrane-distal AMPAR N-terminal domains (NTDs) orchestrate selective routes of heteromeric assembly |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:15456832 Actin/alpha-actinin-dependent transport of AMPA receptors in... | KEEP AS NON CORE | Summary: Endoplasmic reticulum membrane (IDA PMID:15456832; IEA from UniProt subcellular location). Reason: GluA1 is a multi-pass membrane protein synthesized and assembled in the ER; the ER membrane is a biosynthetic transit location, not where the receptor functions. Supporting Evidence: PMID:21317873 the extracellular, membrane-distal AMPAR N-terminal domains (NTDs) orchestrate selective routes of heteromeric assembly |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Endoplasmic reticulum membrane (IDA PMID:15456832; IEA from UniProt subcellular location). Reason: GluA1 is a multi-pass membrane protein synthesized and assembled in the ER; the ER membrane is a biosynthetic transit location, not where the receptor functions. Supporting Evidence: PMID:21317873 the extracellular, membrane-distal AMPAR N-terminal domains (NTDs) orchestrate selective routes of heteromeric assembly |
| GO:0005829 cytosol | IDA PMID:34742997 Deep brain stimulation of the nucleus accumbens shell attenu... | REMOVE | Summary: Cytosol (IDA), from GluR1 detected in the "cytosolic" fraction of a Syn-PER synaptosome preparation from amygdala. Reason: Full text read. The "cytosolic" fraction is simply the non-synaptosomal supernatant of the Syn-PER kit, normalised to actin; it contains non-synaptic membranes. GluA1 is a four-segment integral membrane protein whose topology excludes a soluble cytosolic pool, so the cytosol term is contradicted. The finding (more GluA1 outside synaptosomes after DBS) is real but does not support this location. Supporting Evidence: PMID:34742997 which allows the separation of synaptosomal and cytosolic neuronal fractions from the same samples PMID:34742997 Finally, DBS increased both cytosolic and synaptosomal levels of GluR1, but not GluR2, in the central nucleus of the amygdala but not in other brain regions. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Plasma membrane: GluA1-containing AMPA receptors function at the neuronal plasma membrane. Reason: Core location; surface biotinylation and electrophysiology place functional GluA1 receptors in the plasma membrane, and specifically the postsynaptic density membrane (accepted separately). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. |
| GO:0005886 plasma membrane | IDA PMID:27881773 Novel Roles for the Insulin-Regulated Glucose Transporter-4 ... | ACCEPT | Summary: Plasma membrane: GluA1-containing AMPA receptors function at the neuronal plasma membrane. Reason: Core location; surface biotinylation and electrophysiology place functional GluA1 receptors in the plasma membrane, and specifically the postsynaptic density membrane (accepted separately). Supporting Evidence: PMID:27881773 These effects were accompanied by increased expression of hippocampal AMPA GluR1 subunits file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Plasma membrane: GluA1-containing AMPA receptors function at the neuronal plasma membrane. Reason: Core location; surface biotinylation and electrophysiology place functional GluA1 receptors in the plasma membrane, and specifically the postsynaptic density membrane (accepted separately). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. |
| GO:0005886 plasma membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Plasma membrane: GluA1-containing AMPA receptors function at the neuronal plasma membrane. Reason: Core location; surface biotinylation and electrophysiology place functional GluA1 receptors in the plasma membrane, and specifically the postsynaptic density membrane (accepted separately). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. |
| GO:0005886 plasma membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Plasma membrane: GluA1-containing AMPA receptors function at the neuronal plasma membrane. Reason: Core location; surface biotinylation and electrophysiology place functional GluA1 receptors in the plasma membrane, and specifically the postsynaptic density membrane (accepted separately). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. |
| GO:0005886 plasma membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Plasma membrane: GluA1-containing AMPA receptors function at the neuronal plasma membrane. Reason: Core location; surface biotinylation and electrophysiology place functional GluA1 receptors in the plasma membrane, and specifically the postsynaptic density membrane (accepted separately). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. |
| GO:0005886 plasma membrane | TAS Reactome:R-RNO-9620437 | ACCEPT | Summary: Plasma membrane: GluA1-containing AMPA receptors function at the neuronal plasma membrane. Reason: Core location; surface biotinylation and electrophysiology place functional GluA1 receptors in the plasma membrane, and specifically the postsynaptic density membrane (accepted separately). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0005911 cell-cell junction | IDA PMID:26595655 Synaptic adhesion molecule IgSF11 regulates synaptic transmi... | MARK AS OVER ANNOTATED | Summary: Cell-cell junction (IDA), from GluA1 co-accumulating at IgSF11-mediated cell-cell contacts in transfected heterologous cells. Reason: Full text read: the observation is that overexpressed IgSF11 forms zipper-like contacts between neighbouring COS-7/HEK cells where co-transfected GluA1 and PSD-95 accumulate. This is an artificial reconstitution; in neurons the relevant junction is the glutamatergic synapse, which is annotated separately. Supporting Evidence: PMID:26595655 We next found that IgSF11 proteins expressed in two neighboring cells accumulated at sites of cell-to-cell contacts, forming a zipper-like line where GluA1 and PSD-95 co-accumulated |
| GO:0006811 monoatomic ion transport | IEA GO_REF:0000002 | MODIFY | Summary: Monoatomic ion transport (IEA, InterPro). Reason: Correct but general. GluA1 channels conduct Na+, K+ and Ca2+ across the plasma membrane; refine to GO:0098655 monoatomic cation transmembrane transport (is_a descendant). Proposed replacements: monoatomic cation transmembrane transport Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:1709304 At physiological resting potentials, KA and AMPA elicited inward calcium currents in oocytes expressing GluR1, GluR3, and GluR1 plus GluR3. |
| GO:0007268 chemical synaptic transmission | ISO GO_REF:0000121 | MODIFY | Summary: Chemical synaptic transmission (ISO from mouse Gria1). Reason: Correct but general; AMPA receptors mediate fast glutamatergic transmission. Refine to GO:0035249 synaptic transmission, glutamatergic, an is_a descendant the gene carries by IBA. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: synaptic transmission, glutamatergic Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0007416 synapse assembly | ISO GO_REF:0000121 | MARK AS OVER ANNOTATED | Summary: Synapse assembly (ISO from mouse Gria1). Reason: GluA1 is recruited to and stabilised at existing synapses; synapses form in its absence, and the assembly machinery is the adhesion and scaffold proteins. A requirement of GluA1 for synapse maturation or spine phenotypes in mutant mice is not participation in synapse assembly. Propagation Review Root cause: SOURCE WEAK OR INFERRED Failure modes: SOURCE EVIDENCE WEAK Sources checked: MGI:MGI:95808 SOURCE WEAK OR INFERRED Donor-side annotation reflects a readout or specialised observation that does not establish the claim for GluA1 generally. Supporting Evidence: PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. |
| GO:0007616 long-term memory | IMP PMID:19547753 BDNF activates mTOR to regulate GluR1 expression required fo... | KEEP AS NON CORE | Summary: Long-term memory: blocking training-induced GluR1 translation in dorsal CA1 with antisense oligonucleotides causes amnesia for inhibitory avoidance. Reason: GluA1-containing AMPA receptors are the expression mechanism of hippocampal plasticity that underlies memory; the requirement is well supported (PMID:19547753, full text), but memory is an organism-level outcome downstream of the core synaptic function, so non-core. Supporting Evidence: PMID:19547753 inhibiting GluR1 translation at any of both time points caused amnesia when the animals were tested 24 h after training |
| GO:0007616 long-term memory | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Long-term memory: blocking training-induced GluR1 translation in dorsal CA1 with antisense oligonucleotides causes amnesia for inhibitory avoidance. Reason: GluA1-containing AMPA receptors are the expression mechanism of hippocampal plasticity that underlies memory; the requirement is well supported (PMID:19547753, full text), but memory is an organism-level outcome downstream of the core synaptic function, so non-core. Supporting Evidence: PMID:19547753 inhibiting GluR1 translation at any of both time points caused amnesia when the animals were tested 24 h after training |
| GO:0008021 synaptic vesicle | ISO GO_REF:0000121 | MODIFY | Summary: Synaptic vesicle (ISO from mouse Gria1). Reason: A minor pool of AMPA receptor subunits is presynaptic; the more precise term is GO:0030672 synaptic vesicle membrane (part_of descendant) which the gene also carries by ISO. Non-core either way. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: synaptic vesicle membrane Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0008179 adenylate cyclase binding | IDA PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | MARK AS OVER ANNOTATED | Summary: Adenylate cyclase binding (IDA), from the beta2AR-Gs-adenylyl cyclase-PKA-GluA1 signalling complex. Reason: Adenylyl cyclase is a member of the multiprotein complex assembled around GluA1 via stargazin and PSD-95; co-purification does not show a direct binding activity of GluA1. Full text not available; flagged rather than removed. Supporting Evidence: PMID:19942860 which is linked to the beta(2)AR through stargazin and PSD-95 and their homologues PMID:19942860 Assembly of all proteins involved in the classic beta(2)AR-cAMP cascade into a supramolecular signalling complex |
| GO:0008328 ionotropic glutamate receptor complex | ISO GO_REF:0000121 | MODIFY | Summary: Ionotropic glutamate receptor complex. Reason: Correct but general; GluA1 is a subunit of AMPA-type receptors. Refine to GO:0032281 AMPA glutamate receptor complex (is_a descendant) which the gene carries by IBA, IDA and IPI. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: AMPA glutamate receptor complex Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. file:rat/Gria1/Gria1-uniprot.txt Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 |
| GO:0008328 ionotropic glutamate receptor complex | TAS PMID:11836517 The structure and function of glutamate receptor ion channel... | MODIFY | Summary: Ionotropic glutamate receptor complex. Reason: Correct but general; GluA1 is a subunit of AMPA-type receptors. Refine to GO:0032281 AMPA glutamate receptor complex (is_a descendant) which the gene carries by IBA, IDA and IPI. Proposed replacements: AMPA glutamate receptor complex Supporting Evidence: PMID:11836517 the biochemical and electrophysiological properties of the ionotropic glutamate receptors have been studied extensively PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. |
| GO:0009410 response to xenobiotic stimulus | IEP PMID:19940171 Cannabidiol, a nonpsychotropic component of cannabis, inhibi... | MARK AS OVER ANNOTATED | Summary: Response to xenobiotic stimulus (IEP): GluR1 expression changes in nucleus accumbens with heroin seeking and cannabidiol treatment. Reason: Expression changes in a drug paradigm are readouts; they do not show that GluA1 executes a response to a xenobiotic. Supporting Evidence: PMID:19940171 Discrete disturbances of AMPA GluR1 and cannabinoid type-1 receptor expression observed in the nucleus accumbens associated with stimulus cue-induced heroin seeking were normalized by CBD treatment. |
| GO:0009636 response to toxic substance | IMP PMID:20165912 Regulation of AMPA receptor trafficking by O-glycosylation. | MARK AS OVER ANNOTATED | Summary: Response to toxic substance (IMP), from alloxan (an O-GlcNAc transferase inhibitor) potentiating GluR1 currents, an effect absent in GluR1 S831A. Reason: Alloxan was used as a pharmacological tool to study O-GlcNAcylation-dependent AMPA receptor trafficking; the result concerns regulation of GluA1, not a GluA1-mediated response to a toxic substance. Supporting Evidence: PMID:20165912 Alloxan, an inhibitor of O-GlcNAc transferase, potentiated responses of AMPA receptors composed of the GluR1 subunit expressed in Xenopus oocytes. PMID:20165912 No potentiating effect of alloxan was obtained with mutant GluR1 (S831A) receptor lacking CaMKII phosphorylation site. |
| GO:0009744 response to sucrose | IDA PMID:21425350 Effects of food restriction and sucrose intake on synaptic d... | MARK AS OVER ANNOTATED | Summary: Response to sucrose (IDA): brief sucrose intake increased GluR1 in the nucleus accumbens PSD fraction. Reason: Synaptic GluA1 levels are a readout of reward-related plasticity; this does not show that GluA1 executes a response to sucrose. Supporting Evidence: PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0009897 external side of plasma membrane | IDA PMID:12390532 D1 dopamine receptor stimulation increases GluR1 surface exp... | KEEP AS NON CORE | Summary: External side of plasma membrane (IDA): surface GluA1 detected with N-terminal antibodies on non-permeabilised neurons. Reason: GluA1 has an extracellular N-terminal domain, so surface labelling places part of the protein on the external side of the plasma membrane. True, but the more informative location is the postsynaptic density membrane. Supporting Evidence: PMID:12390532 Regulation of the surface expression of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor subunit GluR1 plays a critical role in long-term potentiation |
| GO:0009897 external side of plasma membrane | IDA PMID:19674091 Nucleus accumbens neurons exhibit synaptic scaling that is o... | KEEP AS NON CORE | Summary: External side of plasma membrane (IDA): surface GluA1 detected with N-terminal antibodies on non-permeabilised neurons. Reason: GluA1 has an extracellular N-terminal domain, so surface labelling places part of the protein on the external side of the plasma membrane. True, but the more informative location is the postsynaptic density membrane. Supporting Evidence: PMID:19674091 Prolonged activity blockade (1-3 days) with an AMPA receptor antagonist increased cell surface (synaptic and extrasynaptic) glutamate receptor 1 (GluR1) and GluR2 but not GluR3 |
| GO:0009986 cell surface | IDA PMID:19321442 PICK1-mediated glutamate receptor subunit 2 (GluR2) traffick... | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:19321442 GluR1 surface expression was unaffected by OGD at all time points tested |
| GO:0009986 cell surface | IDA PMID:23844251 Soluble ICAM-5, a product of activity dependent proteolysis,... | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:23844251 the ICAM-5 ectodomain stimulates an increase in membrane levels of GluA1, but not GluA2, AMPAR subunits |
| GO:0009986 cell surface | IDA PMID:24712995 BDNF contributes to both rapid and homeostatic alterations i... | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:24712995 Immunocytochemical studies showed that acute BDNF treatment increased cell surface GluA1 and GluA2 levels, as well as their co-localization, on NAc neurons. |
| GO:0009986 cell surface | IDA PMID:24884762 Critical role of inflammatory cytokines in impairing biochem... | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:24884762 The tetraethylammonium-induced GluR1 phosphorylation and trafficking were abolished in the hippocampal slices of rats after surgery. |
| GO:0009986 cell surface | IDA PMID:25023288 Endocytic adaptor epidermal growth factor receptor substrate... | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:25023288 Eps15 interacts with AMPARs, which requires Nedd4-mediated GluA1 ubiquitination and the ubiquitin-interacting motif of Eps15. |
| GO:0009986 cell surface | IDA PMID:26088419 Activity-induced synaptic delivery of the GluN2A-containing ... | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:26088419 Bip, an endoplasmic reticulum (ER) chaperone, selectively interacted with GluN2A and mediated the neuronal activity-induced assembly and synaptic incorporation of the GluN2A-containing NMDAR from dendritic ER PMID:19321442 GluR1 surface expression was unaffected by OGD at all time points tested |
| GO:0009986 cell surface | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:19321442 GluR1 surface expression was unaffected by OGD at all time points tested |
| GO:0009986 cell surface | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Cell surface: surface biotinylation and live labelling detect GluA1 at the neuronal surface. Reason: Well supported by many surface-biotinylation studies; it reflects the plasma-membrane receptor pool. Kept as non-core because the informative location is the postsynaptic density membrane. Supporting Evidence: PMID:19321442 GluR1 surface expression was unaffected by OGD at all time points tested |
| GO:0010226 response to lithium ion | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Response to lithium ion: chronic lithium reduces hippocampal synaptic and surface GluR1. Reason: Reduced synaptic GluA1 is the drug effect measured, not a lithium response process executed by GluA1. Supporting Evidence: PMID:15269270 Chronic (but not acute) treatment of rats with therapeutically relevant concentrations of lithium or valproate reduced hippocampal synaptosomal GluR1 levels. |
| GO:0010226 response to lithium ion | IEP PMID:15269270 Modulation of synaptic plasticity by antimanic agents: the r... | MARK AS OVER ANNOTATED | Summary: Response to lithium ion: chronic lithium reduces hippocampal synaptic and surface GluR1. Reason: Reduced synaptic GluA1 is the drug effect measured, not a lithium response process executed by GluA1. Supporting Evidence: PMID:15269270 Chronic (but not acute) treatment of rats with therapeutically relevant concentrations of lithium or valproate reduced hippocampal synaptosomal GluR1 levels. PMID:15269270 The reduction in synaptic GluR1 by lithium and valproate was attributable to a reduction of surface GluR1 distribution onto the neuronal membrane |
| GO:0010628 positive regulation of gene expression | IMP PMID:23460828 Acute BDNF treatment upregulates GluR1-SAP97 and GluR2-GRIP1... | MARK AS OVER ANNOTATED | Summary: Positive regulation of gene expression (IMP): GluR1 knockdown in cortical neurons lowers SAP97 protein levels. Reason: Full text read: SAP97 protein falls when GluR1 is knocked down, consistent with mutual stabilisation of the GluR1-SAP97 complex; the paper notes that BDNF raises GluR1 and SAP97 protein without changing their mRNA. Loss of a binding partner that stabilises SAP97 protein is not regulation of gene expression. Supporting Evidence: PMID:23460828 SAP97 protein levels show a highly significant decline following GluR1-specific dsRNA transduction. PMID:23460828 Our results show that acute BDNF treatment upregulates the interactions between AMPAr subunits (GluR1 and GluR2) with their scaffold proteins SAP97 and GRIP1, respectively |
| GO:0014069 postsynaptic density | IDA PMID:19077125 Extinction of morphine-dependent conditioned behavior is ass... | MODIFY | Summary: Postsynaptic density: GluA1 is enriched in PSD fractions and immunogold-labels PSDs. Reason: Correct but less specific: GluA1 is an integral membrane subunit, so its PSD location is the postsynaptic density membrane, GO:0098839 (part_of descendant of GO:0014069), which the gene carries by IBA, IDA and ISO. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:19077125 Subcellular fractionation techniques were used to analyse the local distribution of AMPA glutamate subunits within the synapse, especially at the postsynaptic density (PSD). |
| GO:0014069 postsynaptic density | IDA PMID:21425350 Effects of food restriction and sucrose intake on synaptic d... | MODIFY | Summary: Postsynaptic density: GluA1 is enriched in PSD fractions and immunogold-labels PSDs. Reason: Correct but less specific: GluA1 is an integral membrane subunit, so its PSD location is the postsynaptic density membrane, GO:0098839 (part_of descendant of GO:0014069), which the gene carries by IBA, IDA and ISO. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0014069 postsynaptic density | IDA PMID:32948689 GRIP1 regulates synaptic plasticity and learning and memory. | MODIFY | Summary: Postsynaptic density: GluA1 is enriched in PSD fractions and immunogold-labels PSDs. Reason: Correct but less specific: GluA1 is an integral membrane subunit, so its PSD location is the postsynaptic density membrane, GO:0098839 (part_of descendant of GO:0014069), which the gene carries by IBA, IDA and ISO. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP |
| GO:0014069 postsynaptic density | ISO GO_REF:0000121 | MODIFY | Summary: Postsynaptic density: GluA1 is enriched in PSD fractions and immunogold-labels PSDs. Reason: Correct but less specific: GluA1 is an integral membrane subunit, so its PSD location is the postsynaptic density membrane, GO:0098839 (part_of descendant of GO:0014069), which the gene carries by IBA, IDA and ISO. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP |
| GO:0015276 ligand-gated monoatomic ion channel activity | IEA GO_REF:0000002 | MODIFY | Summary: Ligand-gated monoatomic ion channel activity (IEA, InterPro). Reason: Correct but general; refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant the gene carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Membrane. Reason: Correct but uninformative; GluA1 functions in the plasma membrane (postsynaptic density membrane). Refine to GO:0005886 plasma membrane, an is_a descendant the gene carries by IBA, IDA, ISS and TAS. Proposed replacements: plasma membrane Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0016020 membrane | ISO GO_REF:0000121 | MODIFY | Summary: Membrane. Reason: Correct but uninformative; GluA1 functions in the plasma membrane (postsynaptic density membrane). Refine to GO:0005886 plasma membrane, an is_a descendant the gene carries by IBA, IDA, ISS and TAS. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: plasma membrane Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0019228 neuronal action potential | IMP PMID:12536214 PKA phosphorylation of AMPA receptor subunits controls synap... | MARK AS OVER ANNOTATED | Summary: Neuronal action potential (IMP), from the study of PKA phosphorylation controlling synaptic AMPA receptor incorporation. Reason: AMPA receptors generate excitatory postsynaptic currents; action-potential generation is carried by voltage-gated Na+/K+ channels. Altered synaptic incorporation of GluA1 changes synaptic strength, not the action potential process itself. Supporting Evidence: PMID:12536214 We found that PKA phosphorylation of the AMPA receptor subunits GluR4 and GluR1 directly controlled the synaptic incorporation of AMPA receptors in organotypic slices from rat hippocampus. |
| GO:0019722 calcium-mediated signaling | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Calcium-mediated signaling (IEA, inferred from calcium channel activity terms). Reason: GluA1-containing GluA2-lacking receptors are Ca2+-permeable, and their Ca2+ influx can trigger downstream signalling, but the downstream calcium-mediated signalling is carried out by calcium sensors and effectors; an inference from channel activity to the signalling process over-reaches. Supporting Evidence: PMID:1709304 At physiological resting potentials, KA and AMPA elicited inward calcium currents in oocytes expressing GluR1, GluR3, and GluR1 plus GluR3. |
| GO:0019865 immunoglobulin binding | IPI PMID:26595655 Synaptic adhesion molecule IgSF11 regulates synaptic transmi... | MODIFY | Summary: Immunoglobulin binding (IPI with IgSF11), from GluA1 co-immunoprecipitating with the synaptic adhesion molecule IgSF11. Reason: The partner IgSF11 is an immunoglobulin-superfamily cell adhesion molecule, not an immunoglobulin (antibody); GO:0019865 is defined as binding to an immunoglobulin, so the term is wrong. The interaction itself is real (rat brain co-IP and COS7 co-expression). Replace with GO:0050839 cell adhesion molecule binding. Proposed replacements: cell adhesion molecule binding Supporting Evidence: PMID:26595655 Intriguingly, IgSF11 formed a coimmunoprecipitable complex with the GluA1 and GluA2 subunits of AMPARs, but not with the GluN1 subunit of NMDARs, in rat brains PMID:26595655 is a dual-binding partner of the postsynaptic scaffolding protein PSD-95 and AMPA glutamate receptors (AMPARs) |
| GO:0019865 immunoglobulin binding | IPI PMID:26595655 Synaptic adhesion molecule IgSF11 regulates synaptic transmi... | MODIFY | Summary: Immunoglobulin binding (IPI with IgSF11), from GluA1 co-immunoprecipitating with the synaptic adhesion molecule IgSF11. Reason: The partner IgSF11 is an immunoglobulin-superfamily cell adhesion molecule, not an immunoglobulin (antibody); GO:0019865 is defined as binding to an immunoglobulin, so the term is wrong. The interaction itself is real (rat brain co-IP and COS7 co-expression). Replace with GO:0050839 cell adhesion molecule binding. Proposed replacements: cell adhesion molecule binding Supporting Evidence: PMID:26595655 Intriguingly, IgSF11 formed a coimmunoprecipitable complex with the GluA1 and GluA2 subunits of AMPARs, but not with the GluN1 subunit of NMDARs, in rat brains PMID:26595655 is a dual-binding partner of the postsynaptic scaffolding protein PSD-95 and AMPA glutamate receptors (AMPARs) |
| GO:0019901 protein kinase binding | IPI PMID:17329210 LTP inhibits LTD in the hippocampus via regulation of GSK3be... | UNDECIDED | Summary: Protein kinase binding (IPI with GSK3beta), from a study of GSK3beta in LTP/LTD interplay. Reason: The abstract (full text not cached) does not describe a GluA1-GSK3beta interaction; the row probably reflects co-immunoprecipitation from hippocampal tissue. A direct kinase-binding activity of GluA1 cannot be verified here. Supporting Evidence: PMID:17329210 Here we show that GSK3beta mediates an interaction between two major forms of synaptic plasticity in the brain |
| GO:0019904 protein domain specific binding | IPI PMID:17194442 Neuronal proteins involved in synaptic targeting of AMPA rec... | MODIFY | Summary: Protein domain specific binding (IPI with SAP97 and stargazin), from co-immunoprecipitation of GluR1 with trafficking partners after antidepressant treatment. Reason: GluA1 binds the PDZ domains of SAP97 through its C-terminal type I PDZ ligand (PMID:16634638). Refine to GO:0030165 PDZ domain binding, an is_a descendant of GO:0019904 that the gene carries by IPI. Proposed replacements: PDZ domain binding Supporting Evidence: PMID:17194442 Paroxetine increased the interaction of GluR1 with Rab4A, and desipramine markedly increased the interaction of GluR1 with SAP97. PMID:16634638 Synaptic delivery of GluR-A (GluR1) subunit-containing glutamate receptors depends on a C-terminal type I PDZ binding motif in GluR-A. |
| GO:0021510 spinal cord development | IEP PMID:19446017 The potential role of phrenic nucleus glutamate receptor sub... | MARK AS OVER ANNOTATED | Summary: Spinal cord development (IEP): GluR1 protein levels in the phrenic nucleus change with postnatal age. Reason: Developmental expression changes do not show that GluA1 executes spinal cord development. Supporting Evidence: PMID:19446017 the protein levels of NR2A and GluR1 in different age rats were assessed via Western blot analysis |
| GO:0021987 cerebral cortex development | IEP PMID:14597197 Brain-derived neurotrophic factor signal enhances and mainta... | MARK AS OVER ANNOTATED | Summary: Cerebral cortex development (IEP): GluR1 protein expression rises during neocortical development, lagging its mRNA. Reason: Developmental expression changes do not show that GluA1 executes cortex development. Supporting Evidence: PMID:14597197 In rat neocortical development, the protein expression of AMPA-type glutamate receptor GluR1 lagged behind its mRNA expression and rather paralleled an increase in PDZ protein levels. |
| GO:0022849 glutamate-gated calcium ion channel activity | IDA PMID:11773314 Voltage and concentration dependence of Ca(2+) permeability ... | ACCEPT | Summary: Glutamate-gated calcium ion channel activity: GluA1 homomers (and GluA2-lacking heteromers) are Ca2+-permeable AMPA receptors. Reason: GluA1 has an unedited Gln at the Q/R site, so GluA1-containing receptors lacking edited GluA2 conduct Ca2+; this was shown in oocytes (PMID:1709304) and quantified for GluR-A(Q) channels (PMID:11773314). These Ca2+-permeable AMPA receptors are transiently inserted after LTP-inducing stimuli and in pathology, so this is a genuine activity of GluA1. Supporting Evidence: PMID:11773314 For GluR-A(Q) channels, P(Ca)/P(Na) derived from all three approaches was concentration independent file:rat/Gria1/Gria1-uniprot.txt Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable |
| GO:0022849 glutamate-gated calcium ion channel activity | IDA PMID:1709304 Ca2+ permeability of KA-AMPA--gated glutamate receptor chann... | ACCEPT | Summary: Glutamate-gated calcium ion channel activity: GluA1 homomers (and GluA2-lacking heteromers) are Ca2+-permeable AMPA receptors. Reason: GluA1 has an unedited Gln at the Q/R site, so GluA1-containing receptors lacking edited GluA2 conduct Ca2+; this was shown in oocytes (PMID:1709304) and quantified for GluR-A(Q) channels (PMID:11773314). These Ca2+-permeable AMPA receptors are transiently inserted after LTP-inducing stimuli and in pathology, so this is a genuine activity of GluA1. Supporting Evidence: PMID:1709304 At physiological resting potentials, KA and AMPA elicited inward calcium currents in oocytes expressing GluR1, GluR3, and GluR1 plus GluR3. PMID:1709304 In contrast, oocytes expressing GluR1 plus GluR2 or GluR3 plus GluR2 showed no such permeability. |
| GO:0022849 glutamate-gated calcium ion channel activity | IEA GO_REF:0000117 | ACCEPT | Summary: Glutamate-gated calcium ion channel activity: GluA1 homomers (and GluA2-lacking heteromers) are Ca2+-permeable AMPA receptors. Reason: GluA1 has an unedited Gln at the Q/R site, so GluA1-containing receptors lacking edited GluA2 conduct Ca2+; this was shown in oocytes (PMID:1709304) and quantified for GluR-A(Q) channels (PMID:11773314). These Ca2+-permeable AMPA receptors are transiently inserted after LTP-inducing stimuli and in pathology, so this is a genuine activity of GluA1. Supporting Evidence: PMID:1709304 At physiological resting potentials, KA and AMPA elicited inward calcium currents in oocytes expressing GluR1, GluR3, and GluR1 plus GluR3. PMID:1709304 In contrast, oocytes expressing GluR1 plus GluR2 or GluR3 plus GluR2 showed no such permeability. PMID:11773314 For GluR-A(Q) channels, P(Ca)/P(Na) derived from all three approaches was concentration independent file:rat/Gria1/Gria1-uniprot.txt Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable |
| GO:0030165 PDZ domain binding | IPI PMID:16634638 Peptide binding and NMR analysis of the interaction between ... | ACCEPT | Summary: PDZ domain binding: the GluA1 C-terminal type I PDZ ligand binds SAP97 PDZ2. Reason: Core trafficking function: the GluA1 C-terminal PDZ ligand binds SAP97 (peptide binding and NMR, PMID:16634638) and the PDZ interaction is required for activity-dependent synaptic delivery (PMID:10731148). Supporting Evidence: PMID:16634638 Synaptic delivery of GluR-A (GluR1) subunit-containing glutamate receptors depends on a C-terminal type I PDZ binding motif in GluR-A. PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. |
| GO:0030425 dendrite | IDA PMID:12629171 Interaction between liprin-alpha and GIT1 is required for AM... | KEEP AS NON CORE | Summary: Dendrite: GluA1 is somatodendritic and abundant in dendrites. Reason: GluA1 traffics through dendrites to spines; a real but less specific location than the postsynaptic density membrane of dendritic spines, where it functions. Supporting Evidence: PMID:12629171 leads to a selective and marked reduction in the dendritic and surface clustering of AMPA receptors in cultured neurons |
| GO:0030425 dendrite | IDA PMID:20032460 Inhibition of calcineurin-mediated endocytosis and alpha-ami... | KEEP AS NON CORE | Summary: Dendrite: GluA1 is somatodendritic and abundant in dendrites. Reason: GluA1 traffics through dendrites to spines; a real but less specific location than the postsynaptic density membrane of dendritic spines, where it functions. Supporting Evidence: PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors |
| GO:0030425 dendrite | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Dendrite: GluA1 is somatodendritic and abundant in dendrites. Reason: GluA1 traffics through dendrites to spines; a real but less specific location than the postsynaptic density membrane of dendritic spines, where it functions. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:12629171 leads to a selective and marked reduction in the dendritic and surface clustering of AMPA receptors in cultured neurons |
| GO:0030425 dendrite | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Dendrite: GluA1 is somatodendritic and abundant in dendrites. Reason: GluA1 traffics through dendrites to spines; a real but less specific location than the postsynaptic density membrane of dendritic spines, where it functions. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:12629171 leads to a selective and marked reduction in the dendritic and surface clustering of AMPA receptors in cultured neurons |
| GO:0030425 dendrite | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Dendrite: GluA1 is somatodendritic and abundant in dendrites. Reason: GluA1 traffics through dendrites to spines; a real but less specific location than the postsynaptic density membrane of dendritic spines, where it functions. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:12629171 leads to a selective and marked reduction in the dendritic and surface clustering of AMPA receptors in cultured neurons |
| GO:0030425 dendrite | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Dendrite: GluA1 is somatodendritic and abundant in dendrites. Reason: GluA1 traffics through dendrites to spines; a real but less specific location than the postsynaptic density membrane of dendritic spines, where it functions. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:12629171 leads to a selective and marked reduction in the dendritic and surface clustering of AMPA receptors in cultured neurons |
| GO:0030672 synaptic vesicle membrane | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Synaptic vesicle membrane (ISO from mouse Gria1). Reason: GluA1 immunogold label is found on presynaptic profiles of glutamatergic terminals; a vesicle membrane pool is plausible but minor and not where GluA1 primarily functions. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0031267 small GTPase binding | IPI PMID:17194442 Neuronal proteins involved in synaptic targeting of AMPA rec... | UNDECIDED | Summary: Small GTPase binding (IPI with Rab4A), from co-immunoprecipitation from hippocampus after paroxetine treatment. Reason: The abstract reports increased GluR1-Rab4A co-immunoprecipitation from tissue; whether GluA1 binds Rab4 directly is not stated and the full text is not cached, so the binding activity cannot be verified. Supporting Evidence: PMID:17194442 Paroxetine increased the interaction of GluR1 with Rab4A, and desipramine markedly increased the interaction of GluR1 with SAP97. |
| GO:0031489 myosin V binding | IPI PMID:16338934 Involvement of myosin Vb in glutamate receptor trafficking. | KEEP AS NON CORE | Summary: Myosin V binding (IPI with myosin Vb). Reason: Myosin Vb associates with GluA1 and its tail domain alters GluA1 somatic accumulation and surface expression (PMID:16338934); a cargo-motor interaction in receptor trafficking, non-core. Supporting Evidence: PMID:16338934 Here we show that myosin Vb is expressed in several neuronal populations and associates with the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate-type glutamate receptor subunit GluR1. PMID:16338934 expression of the tail domain of myosin Vb, but not myosin Va, enhanced GluR1 accumulation in the soma and reduced its surface expression |
| GO:0031594 neuromuscular junction | IDA PMID:19918122 Glutamatergic reinnervation and assembly of glutamatergic sy... | KEEP AS NON CORE | Summary: Neuromuscular junction (IDA): GluR1 partially colocalizes with AChRs at endplates of adult rat muscle reinnervated by glutamatergic spinal axons. Reason: The location is observed in an experimental reinnervation model, not at native cholinergic NMJs; real in that context but peripheral to GluA1 function. Supporting Evidence: PMID:19918122 The alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor subunit GluR1 partially colocalizes with AChRs |
| GO:0031623 receptor internalization | IDA PMID:11100149 Distinct molecular mechanisms and divergent endocytotic path... | KEEP AS NON CORE | Summary: Receptor internalization: AMPA- and insulin-induced AMPA receptor endocytosis depends on GluR1 and GluR2 tail determinants. Reason: GluA1 is the internalized cargo, and sequence determinants in its own cytoplasmic tail (and its ubiquitination, PMID:25023288) direct its internalization; kept as non-core, since the endocytic machinery performs the process. Supporting Evidence: PMID:11100149 insulin- and AMPA-induced AMPA receptor internalization are differentially dependent on protein phosphatases and sequence determinants within the cytoplasmic tails of GluR1 and GluR2 subunits PMID:25023288 Knockdown of Eps15 suppresses the internalization of GluA1 but not the mutant GluA1 that lacks ubiquitination sites |
| GO:0031623 receptor internalization | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Receptor internalization: AMPA- and insulin-induced AMPA receptor endocytosis depends on GluR1 and GluR2 tail determinants. Reason: GluA1 is the internalized cargo, and sequence determinants in its own cytoplasmic tail (and its ubiquitination, PMID:25023288) direct its internalization; kept as non-core, since the endocytic machinery performs the process. Supporting Evidence: PMID:11100149 insulin- and AMPA-induced AMPA receptor internalization are differentially dependent on protein phosphatases and sequence determinants within the cytoplasmic tails of GluR1 and GluR2 subunits PMID:25023288 Knockdown of Eps15 suppresses the internalization of GluA1 but not the mutant GluA1 that lacks ubiquitination sites |
| GO:0031667 response to nutrient levels | IDA PMID:21425350 Effects of food restriction and sucrose intake on synaptic d... | MARK AS OVER ANNOTATED | Summary: Response to nutrient levels (IDA): food restriction increased synaptic AMPA receptor subunits in nucleus accumbens. Reason: Synaptic GluA1 level is the readout measured, not evidence that GluA1 executes a response to nutrient levels. Supporting Evidence: PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0031681 G-protein beta-subunit binding | IDA PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | MARK AS OVER ANNOTATED | Summary: G-protein beta-subunit binding (IDA), from the beta2AR signalling complex containing GluA1. Reason: G protein beta-gamma co-purifies with the multiprotein beta2AR-GluA1 complex linked through stargazin and PSD-95; this does not establish a direct GluA1-Gbeta binding activity. Full text not available; flagged rather than removed. Supporting Evidence: PMID:19942860 which is linked to the beta(2)AR through stargazin and PSD-95 and their homologues PMID:19942860 Assembly of all proteins involved in the classic beta(2)AR-cAMP cascade into a supramolecular signalling complex |
| GO:0031698 beta-2 adrenergic receptor binding | IPI PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | MARK AS OVER ANNOTATED | Summary: Beta-2 adrenergic receptor binding (IPI with Adrb2). Reason: The cited abstracts state that GluA1 is linked to the beta2AR through stargazin and PSD-95 and that both receptors are in a PSD-95/AKAP150/PKA complex; the association is indirect and describes complex membership, not a GluA1 molecular function. Supporting Evidence: PMID:19942860 which is linked to the beta(2)AR through stargazin and PSD-95 and their homologues |
| GO:0031698 beta-2 adrenergic receptor binding | IPI PMID:20395454 Binding of amyloid beta peptide to beta2 adrenergic receptor... | MARK AS OVER ANNOTATED | Summary: Beta-2 adrenergic receptor binding (IPI with Adrb2). Reason: The cited abstracts state that GluA1 is linked to the beta2AR through stargazin and PSD-95 and that both receptors are in a PSD-95/AKAP150/PKA complex; the association is indirect and describes complex membership, not a GluA1 molecular function. Supporting Evidence: PMID:20395454 beta(2)AR and GluR1 also form a complex comprising postsynaptic density protein 95 (PSD95), PKA and its anchor AKAP150, and protein phosphotase 2A (PP2A). |
| GO:0031901 early endosome membrane | IDA PMID:15456832 Actin/alpha-actinin-dependent transport of AMPA receptors in... | KEEP AS NON CORE | Summary: Early endosome membrane: GluA1 colocalizes with PDLIM4 (RIL) in early endosomes. Reason: A trafficking intermediate location, well supported (UniProt ECO:0000269 from PMID:15456832), non-core. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Colocalizes with PDLIM4 in early endosomes PMID:15456832 We show that RIL binds to the AMPA glutamate receptor subunit GluR-A C-terminal peptide via its LIM domain and to alpha-actinin via its PDZ domain. |
| GO:0031901 early endosome membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Early endosome membrane: GluA1 colocalizes with PDLIM4 (RIL) in early endosomes. Reason: A trafficking intermediate location, well supported (UniProt ECO:0000269 from PMID:15456832), non-core. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Colocalizes with PDLIM4 in early endosomes PMID:15456832 We show that RIL binds to the AMPA glutamate receptor subunit GluR-A C-terminal peptide via its LIM domain and to alpha-actinin via its PDZ domain. |
| GO:0032279 asymmetric synapse | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | KEEP AS NON CORE | Summary: Asymmetric synapse (IDA): AMPAR immunogold (GluR1/2/3 combined antibody) at asymmetric synapses of rat sensory cortex. Reason: AMPA receptors are concentrated at asymmetric (excitatory) synapses; the antibody did not resolve GluA1 from GluA2/3, but the location is consistent with GluA1 biology. The informative term is glutamatergic synapse/PSD membrane. Supporting Evidence: PMID:12077196 we used dual immunolabeling and electron microscopy to examine the distribution of alpha7nAChR relative to AMPAR (GluR1, GluR2, and GluR3 subunits combined) at excitatory synapses |
| GO:0032281 AMPA glutamate receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: AMPA glutamate receptor complex: GluA1 assembles with GluA2-4 and auxiliary TARP and cornichon subunits. Reason: Core complex membership: proteomics of native rat AMPA receptors (PMID:19265014) and the GluA1/2-TARP gamma-8 cryo-EM structure (PMID:30872532). Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. file:rat/Gria1/Gria1-uniprot.txt Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 |
| GO:0032281 AMPA glutamate receptor complex | IDA PMID:19265014 Functional proteomics identify cornichon proteins as auxilia... | ACCEPT | Summary: AMPA glutamate receptor complex: GluA1 assembles with GluA2-4 and auxiliary TARP and cornichon subunits. Reason: Core complex membership: proteomics of native rat AMPA receptors (PMID:19265014) and the GluA1/2-TARP gamma-8 cryo-EM structure (PMID:30872532). Supporting Evidence: PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. |
| GO:0032281 AMPA glutamate receptor complex | IEA GO_REF:0000120 | ACCEPT | Summary: AMPA glutamate receptor complex: GluA1 assembles with GluA2-4 and auxiliary TARP and cornichon subunits. Reason: Core complex membership: proteomics of native rat AMPA receptors (PMID:19265014) and the GluA1/2-TARP gamma-8 cryo-EM structure (PMID:30872532). Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. file:rat/Gria1/Gria1-uniprot.txt Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 |
| GO:0032281 AMPA glutamate receptor complex | IPI PMID:30872532 Architecture of the heteromeric GluA1/2 AMPA receptor in com... | ACCEPT | Summary: AMPA glutamate receptor complex: GluA1 assembles with GluA2-4 and auxiliary TARP and cornichon subunits. Reason: Core complex membership: proteomics of native rat AMPA receptors (PMID:19265014) and the GluA1/2-TARP gamma-8 cryo-EM structure (PMID:30872532). Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. |
| GO:0032281 AMPA glutamate receptor complex | ISO GO_REF:0000121 | ACCEPT | Summary: AMPA glutamate receptor complex: GluA1 assembles with GluA2-4 and auxiliary TARP and cornichon subunits. Reason: Core complex membership: proteomics of native rat AMPA receptors (PMID:19265014) and the GluA1/2-TARP gamma-8 cryo-EM structure (PMID:30872532). Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. file:rat/Gria1/Gria1-uniprot.txt Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 |
| GO:0032281 AMPA glutamate receptor complex | ISO GO_REF:0000121 | ACCEPT | Summary: AMPA glutamate receptor complex: GluA1 assembles with GluA2-4 and auxiliary TARP and cornichon subunits. Reason: Core complex membership: proteomics of native rat AMPA receptors (PMID:19265014) and the GluA1/2-TARP gamma-8 cryo-EM structure (PMID:30872532). Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. PMID:19265014 Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. file:rat/Gria1/Gria1-uniprot.txt Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8 |
| GO:0032355 response to estradiol | IEP PMID:19596275 Estrogen receptor alpha and beta specific agonists regulate ... | MARK AS OVER ANNOTATED | Summary: Response to estradiol (IEP): estradiol and ER agonists increased GluR1 immunoreactivity in CA1 stratum radiatum. Reason: An expression change is a readout; it does not show that GluA1 executes an estradiol response. Supporting Evidence: PMID:19596275 In the stratum radiatum, estradiol, DPN, and PPT increased PSD-95 and AMPA-type glutamate receptor subunit GluR1. |
| GO:0032590 dendrite membrane | IDA PMID:11931740 Interaction between GRIP and liprin-alpha/SYD2 is required f... | KEEP AS NON CORE | Summary: Dendrite membrane. Reason: GluA1 receptors are present in the dendritic plasma membrane, including extrasynaptic pools that feed synapses; real but less informative than postsynaptic density membrane. Supporting Evidence: PMID:11931740 Interaction with the multi-PDZ protein GRIP is required for the synaptic targeting of AMPA receptors |
| GO:0032590 dendrite membrane | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Dendrite membrane. Reason: GluA1 receptors are present in the dendritic plasma membrane, including extrasynaptic pools that feed synapses; real but less informative than postsynaptic density membrane. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:11931740 Interaction with the multi-PDZ protein GRIP is required for the synaptic targeting of AMPA receptors |
| GO:0032591 dendritic spine membrane | IEA GO_REF:0000107 | ACCEPT | Summary: Dendritic spine membrane. Reason: GluA1-containing receptors are inserted into the spine plasma membrane during LTP; this is where the receptor functions, together with the PSD membrane. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines |
| GO:0032591 dendritic spine membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Dendritic spine membrane. Reason: GluA1-containing receptors are inserted into the spine plasma membrane during LTP; this is where the receptor functions, together with the PSD membrane. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines |
| GO:0032591 dendritic spine membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Dendritic spine membrane. Reason: GluA1-containing receptors are inserted into the spine plasma membrane during LTP; this is where the receptor functions, together with the PSD membrane. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines |
| GO:0032809 neuronal cell body membrane | IDA PMID:10985351 Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in ... | KEEP AS NON CORE | Summary: Neuronal cell body membrane (IDA, PMID:10985351, abstract only). Reason: GluA1 is somatodendritic and present in somatic plasma membrane; the cached abstract concerns GluR2 trafficking, but the location is consistent with GluA1 biology, so the curator is deferred to. Non-core. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0032991 protein-containing complex | IDA PMID:17329210 LTP inhibits LTD in the hippocampus via regulation of GSK3be... | TOO GENERAL | Summary: Protein-containing complex (IDA). Reason: True but uninformative: GluA1 is in the AMPA glutamate receptor complex (GO:0032281), accepted in this review, which entails this term. Supporting Evidence: PMID:17329210 Here we show that GSK3beta mediates an interaction between two major forms of synaptic plasticity in the brain |
| GO:0034220 monoatomic ion transmembrane transport | IEA GO_REF:0000120 | MODIFY | Summary: Monoatomic ion transmembrane transport (IEA, from channel activity terms). Reason: Correct but general; GluA1 receptors are cation-selective. Refine to GO:0098655 monoatomic cation transmembrane transport (is_a descendant). Proposed replacements: monoatomic cation transmembrane transport Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:1709304 At physiological resting potentials, KA and AMPA elicited inward calcium currents in oocytes expressing GluR1, GluR3, and GluR1 plus GluR3. |
| GO:0034765 regulation of monoatomic ion transmembrane transport | IMP PMID:21613507 Reinforcement-related regulation of AMPA glutamate receptor ... | MARK AS OVER ANNOTATED | Summary: Regulation of monoatomic ion transmembrane transport (IMP): VTA overexpression of GluR1 increased AMPA-evoked inward rectification. Reason: GluA1 is the channel that carries the current; overexpressing it changes receptor composition (more GluA2-lacking, inwardly rectifying receptors) rather than regulating a separate transport process. Its transport role is captured by channel activity and cation transmembrane transport. Supporting Evidence: PMID:21613507 Overexpression of GluR1(WT) in rat VTA primarily infected dopamine neurons (75%) and increased AMPA receptor-mediated membrane rectification in these neurons with AMPA application. |
| GO:0035235 ionotropic glutamate receptor signaling pathway | NAS PMID:30872532 Architecture of the heteromeric GluA1/2 AMPA receptor in com... | ACCEPT | Summary: Ionotropic glutamate receptor signaling pathway (NAS), from the GluA1/2-TARP gamma-8 structure paper. Reason: GluA1 is a glutamate-binding, ion-conducting subunit of the receptor that initiates this pathway. Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0035249 synaptic transmission, glutamatergic | IBA GO_REF:0000033 | ACCEPT | Summary: Synaptic transmission, glutamatergic. Reason: Core process: AMPA receptors mediate most fast excitatory glutamatergic transmission, and GluA1/GluA2 receptors are the principal hippocampal synaptic AMPARs. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. |
| GO:0035249 synaptic transmission, glutamatergic | NAS PMID:15269270 Modulation of synaptic plasticity by antimanic agents: the r... | ACCEPT | Summary: Synaptic transmission, glutamatergic. Reason: Core process: AMPA receptors mediate most fast excitatory glutamatergic transmission, and GluA1/GluA2 receptors are the principal hippocampal synaptic AMPARs. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. |
| GO:0035254 glutamate receptor binding | IPI PMID:21639859 Crystal structure of the glutamate receptor GluA1 N-terminal... | KEEP AS NON CORE | Summary: Glutamate receptor binding (IPI with GluA2), from GluA1 N-terminal domain associations. Reason: GluA1 NTD heterodimerizes with GluA2 NTD during receptor assembly; this is subunit assembly within the AMPA receptor complex rather than a separate binding function, kept as non-core. Supporting Evidence: PMID:21639859 analysis of the crystal lattice of GluA1-ATD suggests a novel mechanism by which the ATD might participate in inter-tetramer AMPAR clustering PMID:21317873 the extracellular, membrane-distal AMPAR N-terminal domains (NTDs) orchestrate selective routes of heteromeric assembly |
| GO:0036477 somatodendritic compartment | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Somatodendritic compartment (ISO from mouse). Reason: UniProt notes a somatodendritic localization with exclusion from axons; accurate but general. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0038023 signaling receptor activity | IEA GO_REF:0000002 | MODIFY | Summary: Signaling receptor activity (IEA, InterPro). Reason: Correct but general; GluA1 is an ionotropic AMPA receptor subunit. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant the gene carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:2166337 Functional expression of the cDNAs in cultured mammalian cells generated receptors displaying alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-selective binding pharmacology (AMPA = quisqualate greater than glutamate greater than kainate) as well as cation channels gated by glutamate, AMPA, and kainate file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0042220 response to cocaine | IEP PMID:15548228 A single high dose of cocaine induces behavioural sensitizat... | MARK AS OVER ANNOTATED | Summary: Response to cocaine (IEP): cocaine exposure or self-administration changes GluR1 mRNA or protein in VTA and other regions. Reason: Expression changes in drug paradigms are readouts of neuroadaptation; they do not show that GluA1 executes a response to cocaine. Supporting Evidence: PMID:15548228 a single, behavioural sensitizing dose of cocaine is sufficient to induce changes in the mRNA levels of growth-associated protein 43 (GAP-43) |
| GO:0042220 response to cocaine | IEP PMID:20600170 Electrical stimulation of the lateral habenula produces endu... | MARK AS OVER ANNOTATED | Summary: Response to cocaine (IEP): cocaine exposure or self-administration changes GluR1 mRNA or protein in VTA and other regions. Reason: Expression changes in drug paradigms are readouts of neuroadaptation; they do not show that GluA1 executes a response to cocaine. Supporting Evidence: PMID:20600170 In the ventral tegmental area, cocaine self-administration elevated glutamatergic receptor subunits NR1 and GluR1 and scaffolding protein PSD95 |
| GO:0042220 response to cocaine | IEP PMID:21613507 Reinforcement-related regulation of AMPA glutamate receptor ... | MARK AS OVER ANNOTATED | Summary: Response to cocaine (IEP): cocaine exposure or self-administration changes GluR1 mRNA or protein in VTA and other regions. Reason: Expression changes in drug paradigms are readouts of neuroadaptation; they do not show that GluA1 executes a response to cocaine. Supporting Evidence: PMID:21613507 daily intravenous cocaine self-administration, but not passive cocaine administration, induces dynamic upregulation of the AMPA glutamate receptor subunits GluR1 and GluR2 in the ventral tegmental area (VTA) of rats |
| GO:0042734 presynaptic membrane | IDA PMID:16903873 Ultrastructural localisation and differential agonist-induce... | KEEP AS NON CORE | Summary: Presynaptic membrane: GluR1 immunoreactivity in presynaptic active-zone fractions and on presynaptic profiles. Reason: A minor presynaptic GluA1 pool is supported by synaptosome subfractionation and immunogold; real but not the main site of function. Supporting Evidence: PMID:16903873 All of the subunits were enriched in the postsynaptic fraction but were also present in the presynaptic and non-synaptic synaptosome fractions. |
| GO:0042734 presynaptic membrane | IEP PMID:16903873 Ultrastructural localisation and differential agonist-induce... | KEEP AS NON CORE | Summary: Presynaptic membrane: GluR1 immunoreactivity in presynaptic active-zone fractions and on presynaptic profiles. Reason: A minor presynaptic GluA1 pool is supported by synaptosome subfractionation and immunogold; real but not the main site of function. Supporting Evidence: PMID:16903873 All of the subunits were enriched in the postsynaptic fraction but were also present in the presynaptic and non-synaptic synaptosome fractions. PMID:16903873 NMDA treatment decreased postsynaptic GluR1, GluR2 and GluR6/7 but increased presynaptic levels of these subunits. |
| GO:0042802 identical protein binding | IPI PMID:19461580 Crystal structure and association behaviour of the GluR2 ami... | KEEP AS NON CORE | Summary: Identical protein binding: GluA1 NTDs self-associate (homodimers) during receptor assembly. Reason: Homo-association of the GluA1 NTD is part of tetramer assembly; it is real (crystal structure, biophysics) but is subunit assembly rather than a separate function. Supporting Evidence: PMID:19461580 Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers |
| GO:0042802 identical protein binding | IPI PMID:21317873 Subunit-selective N-terminal domain associations organize th... | KEEP AS NON CORE | Summary: Identical protein binding: GluA1 NTDs self-associate (homodimers) during receptor assembly. Reason: Homo-association of the GluA1 NTD is part of tetramer assembly; it is real (crystal structure, biophysics) but is subunit assembly rather than a separate function. Supporting Evidence: PMID:21317873 the extracellular, membrane-distal AMPAR N-terminal domains (NTDs) orchestrate selective routes of heteromeric assembly |
| GO:0042802 identical protein binding | IPI PMID:21639859 Crystal structure of the glutamate receptor GluA1 N-terminal... | KEEP AS NON CORE | Summary: Identical protein binding: GluA1 NTDs self-associate (homodimers) during receptor assembly. Reason: Homo-association of the GluA1 NTD is part of tetramer assembly; it is real (crystal structure, biophysics) but is subunit assembly rather than a separate function. Supporting Evidence: PMID:21639859 analysis of the crystal lattice of GluA1-ATD suggests a novel mechanism by which the ATD might participate in inter-tetramer AMPAR clustering |
| GO:0043005 neuron projection | IDA PMID:12390532 D1 dopamine receptor stimulation increases GluR1 surface exp... | MODIFY | Summary: Neuron projection. Reason: Correct but general; GluA1 is somatodendritic and excluded from axons, so the projection is the dendrite. Refine to GO:0030425 dendrite, an is_a descendant the gene carries by IDA, ISO and ISS. Proposed replacements: dendrite Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043005 neuron projection | ISO GO_REF:0000121 | MODIFY | Summary: Neuron projection. Reason: Correct but general; GluA1 is somatodendritic and excluded from axons, so the projection is the dendrite. Refine to GO:0030425 dendrite, an is_a descendant the gene carries by IDA, ISO and ISS. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: dendrite Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043025 neuronal cell body | IDA PMID:11100149 Distinct molecular mechanisms and divergent endocytotic path... | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: PMID:11100149 insulin- and AMPA-induced AMPA receptor internalization are differentially dependent on protein phosphatases and sequence determinants within the cytoplasmic tails of GluR1 and GluR2 subunits file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043025 neuronal cell body | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: PMID:12077196 we used dual immunolabeling and electron microscopy to examine the distribution of alpha7nAChR relative to AMPAR (GluR1, GluR2, and GluR3 subunits combined) at excitatory synapses file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043025 neuronal cell body | IDA PMID:20032460 Inhibition of calcineurin-mediated endocytosis and alpha-ami... | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043025 neuronal cell body | IDA PMID:20802490 Plk2 attachment to NSF induces homeostatic removal of GluA2 ... | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: PMID:20802490 increased ratio of surface GluA1 to GluA2 subunits file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043025 neuronal cell body | IDA PMID:25023288 Endocytic adaptor epidermal growth factor receptor substrate... | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: PMID:25023288 Eps15 interacts with AMPARs, which requires Nedd4-mediated GluA1 ubiquitination and the ubiquitin-interacting motif of Eps15. file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043025 neuronal cell body | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:16338934 expression of the tail domain of myosin Vb, but not myosin Va, enhanced GluR1 accumulation in the soma and reduced its surface expression |
| GO:0043025 neuronal cell body | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:16338934 expression of the tail domain of myosin Vb, but not myosin Va, enhanced GluR1 accumulation in the soma and reduced its surface expression |
| GO:0043025 neuronal cell body | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:16338934 expression of the tail domain of myosin Vb, but not myosin Va, enhanced GluR1 accumulation in the soma and reduced its surface expression |
| GO:0043025 neuronal cell body | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Neuronal cell body. Reason: GluA1 is synthesized in and present at the soma (somatodendritic localization); a real but non-core location. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons PMID:16338934 expression of the tail domain of myosin Vb, but not myosin Va, enhanced GluR1 accumulation in the soma and reduced its surface expression |
| GO:0043197 dendritic spine | IBA GO_REF:0000033 | ACCEPT | Summary: Dendritic spine: GluA1 localizes to spines and is delivered there during LTP. Reason: Core location: GluA1-containing AMPA receptors are concentrated in dendritic spines, where glutamatergic synapses form. Supporting Evidence: PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors PMID:19208802 GEF-H1 is enriched in the postsynaptic density and is colocalized with GluR1 at spines. |
| GO:0043197 dendritic spine | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | ACCEPT | Summary: Dendritic spine: GluA1 localizes to spines and is delivered there during LTP. Reason: Core location: GluA1-containing AMPA receptors are concentrated in dendritic spines, where glutamatergic synapses form. Supporting Evidence: PMID:12077196 we used dual immunolabeling and electron microscopy to examine the distribution of alpha7nAChR relative to AMPAR (GluR1, GluR2, and GluR3 subunits combined) at excitatory synapses |
| GO:0043197 dendritic spine | IDA PMID:16338934 Involvement of myosin Vb in glutamate receptor trafficking. | ACCEPT | Summary: Dendritic spine: GluA1 localizes to spines and is delivered there during LTP. Reason: Core location: GluA1-containing AMPA receptors are concentrated in dendritic spines, where glutamatergic synapses form. Supporting Evidence: PMID:16338934 Here we show that myosin Vb is expressed in several neuronal populations and associates with the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate-type glutamate receptor subunit GluR1. |
| GO:0043197 dendritic spine | IDA PMID:20032460 Inhibition of calcineurin-mediated endocytosis and alpha-ami... | ACCEPT | Summary: Dendritic spine: GluA1 localizes to spines and is delivered there during LTP. Reason: Core location: GluA1-containing AMPA receptors are concentrated in dendritic spines, where glutamatergic synapses form. Supporting Evidence: PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors PMID:19208802 GEF-H1 is enriched in the postsynaptic density and is colocalized with GluR1 at spines. |
| GO:0043197 dendritic spine | IDA PMID:23844251 Soluble ICAM-5, a product of activity dependent proteolysis,... | ACCEPT | Summary: Dendritic spine: GluA1 localizes to spines and is delivered there during LTP. Reason: Core location: GluA1-containing AMPA receptors are concentrated in dendritic spines, where glutamatergic synapses form. Supporting Evidence: PMID:23844251 the ICAM-5 ectodomain stimulates an increase in membrane levels of GluA1, but not GluA2, AMPAR subunits |
| GO:0043197 dendritic spine | IEA GO_REF:0000120 | ACCEPT | Summary: Dendritic spine: GluA1 localizes to spines and is delivered there during LTP. Reason: Core location: GluA1-containing AMPA receptors are concentrated in dendritic spines, where glutamatergic synapses form. Supporting Evidence: PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors PMID:19208802 GEF-H1 is enriched in the postsynaptic density and is colocalized with GluR1 at spines. |
| GO:0043197 dendritic spine | ISO GO_REF:0000121 | ACCEPT | Summary: Dendritic spine: GluA1 localizes to spines and is delivered there during LTP. Reason: Core location: GluA1-containing AMPA receptors are concentrated in dendritic spines, where glutamatergic synapses form. Supporting Evidence: PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines PMID:20032460 Immunocolocalization experiments confirmed that ADDL binding occurs in dendritic spines that express surface AMPA receptors PMID:19208802 GEF-H1 is enriched in the postsynaptic density and is colocalized with GluR1 at spines. |
| GO:0043198 dendritic shaft | IDA PMID:11100149 Distinct molecular mechanisms and divergent endocytotic path... | KEEP AS NON CORE | Summary: Dendritic shaft. Reason: GluA1 is present in dendritic shafts (extrasynaptic and shaft-synapse pools); real but not the main functional site. Supporting Evidence: PMID:11100149 insulin- and AMPA-induced AMPA receptor internalization are differentially dependent on protein phosphatases and sequence determinants within the cytoplasmic tails of GluR1 and GluR2 subunits file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043198 dendritic shaft | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | KEEP AS NON CORE | Summary: Dendritic shaft. Reason: GluA1 is present in dendritic shafts (extrasynaptic and shaft-synapse pools); real but not the main functional site. Supporting Evidence: PMID:12077196 we used dual immunolabeling and electron microscopy to examine the distribution of alpha7nAChR relative to AMPAR (GluR1, GluR2, and GluR3 subunits combined) at excitatory synapses |
| GO:0043198 dendritic shaft | IDA PMID:19160501 Serine phosphorylation of ephrinB2 regulates trafficking of ... | KEEP AS NON CORE | Summary: Dendritic shaft. Reason: GluA1 is present in dendritic shafts (extrasynaptic and shaft-synapse pools); real but not the main functional site. Supporting Evidence: PMID:19160501 EphrinB2 signaling is critical for the stabilization of AMPA receptors at the cellular membrane. |
| GO:0043198 dendritic shaft | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Dendritic shaft. Reason: GluA1 is present in dendritic shafts (extrasynaptic and shaft-synapse pools); real but not the main functional site. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0043278 response to morphine | IEP PMID:24201449 Region-specific alterations in glutamate receptor 1 phosphor... | MARK AS OVER ANNOTATED | Summary: Response to morphine: GluA1 levels or phosphorylation change in morphine paradigms, and GluA1 phosphorylation is required for context-dependent sensitization. Reason: Expression and phosphorylation changes are readouts; the IMP result shows that GluA1 phosphorylation is needed for drug-associated behavioural plasticity, which is the synaptic plasticity role of GluA1 (captured by LTP and glutamatergic transmission), not a "response to morphine" executed by GluA1. Supporting Evidence: PMID:24201449 Phosphorylation of GluR1 at Ser845, but not Ser831, increases in the nucleus accumbens and central amygdala from 1 to 10 days of withdrawal |
| GO:0043278 response to morphine | IEP PMID:25716866 Persistent pain maintains morphine-seeking behavior after mo... | MARK AS OVER ANNOTATED | Summary: Response to morphine: GluA1 levels or phosphorylation change in morphine paradigms, and GluA1 phosphorylation is required for context-dependent sensitization. Reason: Expression and phosphorylation changes are readouts; the IMP result shows that GluA1 phosphorylation is needed for drug-associated behavioural plasticity, which is the synaptic plasticity role of GluA1 (captured by LTP and glutamatergic transmission), not a "response to morphine" executed by GluA1. Supporting Evidence: PMID:25716866 proteins of GluA1 subunits of glutamate AMPA receptors were upregulated during morphine withdrawal, and viral knockdown of CeA GluA1 eliminated the morphine-seeking behavior in withdrawn rats of the pain group |
| GO:0043278 response to morphine | IEP PMID:32717192 Corydaline and l-tetrahydropalmatine attenuate morphine-indu... | MARK AS OVER ANNOTATED | Summary: Response to morphine: GluA1 levels or phosphorylation change in morphine paradigms, and GluA1 phosphorylation is required for context-dependent sensitization. Reason: Expression and phosphorylation changes are readouts; the IMP result shows that GluA1 phosphorylation is needed for drug-associated behavioural plasticity, which is the synaptic plasticity role of GluA1 (captured by LTP and glutamatergic transmission), not a "response to morphine" executed by GluA1. Supporting Evidence: PMID:32717192 Western-blot immunoreactive assays were used to evaluate morphine-induced changes in dopamine D2 receptor and GluA1 AMPA receptor and GluA2 AMPA receptor expression in the brain of rats |
| GO:0043278 response to morphine | IMP PMID:22072679 Hippocampal GluA1-containing AMPA receptors mediate context-... | MARK AS OVER ANNOTATED | Summary: Response to morphine: GluA1 levels or phosphorylation change in morphine paradigms, and GluA1 phosphorylation is required for context-dependent sensitization. Reason: Expression and phosphorylation changes are readouts; the IMP result shows that GluA1 phosphorylation is needed for drug-associated behavioural plasticity, which is the synaptic plasticity role of GluA1 (captured by LTP and glutamatergic transmission), not a "response to morphine" executed by GluA1. Supporting Evidence: PMID:22072679 phosphorylation of GluA1 AMPAR subunit plays a critical role in the acquisition and expression of context-dependent behavioral sensitization |
| GO:0043434 response to peptide hormone | IEP PMID:20554878 Regulation of nucleus accumbens activity by the hypothalamic... | MARK AS OVER ANNOTATED | Summary: Response to peptide hormone (IEP): melanin-concentrating hormone lowers GluR1 Ser845 phosphorylation and surface GluR1 in nucleus accumbens shell. Reason: GluA1 is the downstream target whose phosphorylation and surface level change; it does not execute the hormone response. Supporting Evidence: PMID:20554878 A reduction of phosphorylation of GluR1 at serine 845 (pSer(845)) is shown to occur after both pharmacological and genetic manipulations of MCHR1 activity. |
| GO:0044297 cell body | ISO GO_REF:0000121 | MODIFY | Summary: Cell body (ISO from mouse). Reason: Correct but general; refine to GO:0043025 neuronal cell body, an is_a descendant the gene carries by IDA and ISO. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: neuronal cell body Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0044308 axonal spine | ISO GO_REF:0000121 | MARK AS OVER ANNOTATED | Summary: Axonal spine (ISO from mouse Gria1). Reason: UniProt (by similarity) describes GluA1 as somatodendritic and excluded from axons; an axonal-spine location for GluA1 is not supported by the rat literature reviewed here and is likely an over-propagation of a specialised observation. Propagation Review Root cause: SOURCE WEAK OR INFERRED Failure modes: SOURCE EVIDENCE WEAK Sources checked: MGI:MGI:95808 SOURCE WEAK OR INFERRED Donor-side annotation reflects a readout or specialised observation that does not establish the claim for GluA1 generally. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0044309 neuron spine | IDA PMID:10985351 Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in ... | MODIFY | Summary: Neuron spine. Reason: Correct but general; the spines carrying GluA1 are dendritic spines. Refine to GO:0043197 dendritic spine, an is_a descendant the gene carries by IBA and IDA. Proposed replacements: dendritic spine Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Displays a somatodendritic localization and is excluded from axons in neurons |
| GO:0044309 neuron spine | IDA PMID:20083202 Regulation of synaptic structure and function by palmitoylat... | MODIFY | Summary: Neuron spine. Reason: Correct but general; the spines carrying GluA1 are dendritic spines. Refine to GO:0043197 dendritic spine, an is_a descendant the gene carries by IBA and IDA. Proposed replacements: dendritic spine Supporting Evidence: PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines |
| GO:0044309 neuron spine | ISO GO_REF:0000121 | MODIFY | Summary: Neuron spine. Reason: Correct but general; the spines carrying GluA1 are dendritic spines. Refine to GO:0043197 dendritic spine, an is_a descendant the gene carries by IBA and IDA. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: dendritic spine Supporting Evidence: PMID:20083202 GluR1 staining co-localized well with pABP-L in neurons and both were readily detected in spines |
| GO:0045202 synapse | IDA PMID:10939335 Targeting of PKA to glutamate receptors through a MAGUK-AKAP... | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:10939335 Two classes of binding proteins organize these complexes: the MAGUK proteins that cluster glutamate receptors and AKAPs that anchor kinases and phosphatases. |
| GO:0045202 synapse | IDA PMID:15681343 Control of excitatory and inhibitory synapse formation by ne... | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045202 synapse | IDA PMID:23345231 Central amygdala GluA1 facilitates associative learning of o... | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:23345231 Whole-cell recording revealed enhanced electrophysiological properties of postsynaptic GluA2-lacking AMPA receptors in adenoviral GluA1-infected CeA neurons. |
| GO:0045202 synapse | IDA PMID:25129673 Impact of combined prenatal ethanol and prenatal stress expo... | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:25129673 TTTC significantly elevated both synaptosomal GluA1 and GluA2 subunit expression relative to the UPC group in control offspring |
| GO:0045202 synapse | IDA PMID:34742997 Deep brain stimulation of the nucleus accumbens shell attenu... | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:34742997 Finally, DBS increased both cytosolic and synaptosomal levels of GluR1, but not GluR2, in the central nucleus of the amygdala but not in other brain regions. |
| GO:0045202 synapse | IEA GO_REF:0000044 | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045202 synapse | IMP PMID:12536214 PKA phosphorylation of AMPA receptor subunits controls synap... | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:12536214 We found that PKA phosphorylation of the AMPA receptor subunits GluR4 and GluR1 directly controlled the synaptic incorporation of AMPA receptors in organotypic slices from rat hippocampus. |
| GO:0045202 synapse | ISO GO_REF:0000121 | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045202 synapse | ISS GO_REF:0000024 | MODIFY | Summary: Synapse. Reason: Correct but general; GluA1 functions at glutamatergic synapses. Refine to GO:0098978 glutamatergic synapse, an is_a descendant the gene carries by IDA and ISO. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P23818 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045211 postsynaptic membrane | IDA PMID:16903873 Ultrastructural localisation and differential agonist-induce... | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:16903873 All of the subunits were enriched in the postsynaptic fraction but were also present in the presynaptic and non-synaptic synaptosome fractions. |
| GO:0045211 postsynaptic membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045211 postsynaptic membrane | IEP PMID:16903873 Ultrastructural localisation and differential agonist-induce... | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:16903873 All of the subunits were enriched in the postsynaptic fraction but were also present in the presynaptic and non-synaptic synaptosome fractions. PMID:16903873 NMDA treatment decreased postsynaptic GluR1, GluR2 and GluR6/7 but increased presynaptic levels of these subunits. |
| GO:0045211 postsynaptic membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045211 postsynaptic membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045211 postsynaptic membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045211 postsynaptic membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0045211 postsynaptic membrane | NAS PMID:17506699 The cell biology of synaptic plasticity: AMPA receptor traff... | ACCEPT | Summary: Postsynaptic membrane. Reason: Core location: GluA1-containing AMPA receptors are inserted into the postsynaptic plasma membrane, where they mediate excitatory currents. Supporting Evidence: PMID:17506699 This is particularly evident in the trafficking and regulation of membrane proteins to and from synapses PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. |
| GO:0045471 response to ethanol | IEP PMID:21041654 Role for mammalian target of rapamycin complex 1 signaling i... | MARK AS OVER ANNOTATED | Summary: Response to ethanol (IEP): GluA1 levels change in alcohol-drinking or prenatal-ethanol paradigms. Reason: Expression changes in ethanol paradigms are readouts; they do not show that GluA1 executes an ethanol response. Supporting Evidence: PMID:21041654 the protein expression levels of GluR1 and Homer, two synaptic proteins whose translation has been shown to be modulated by mTORC1, are up-regulated in the NAc of rodents with a history of excessive alcohol consumption |
| GO:0045471 response to ethanol | IEP PMID:25129673 Impact of combined prenatal ethanol and prenatal stress expo... | MARK AS OVER ANNOTATED | Summary: Response to ethanol (IEP): GluA1 levels change in alcohol-drinking or prenatal-ethanol paradigms. Reason: Expression changes in ethanol paradigms are readouts; they do not show that GluA1 executes an ethanol response. Supporting Evidence: PMID:25129673 TTTC significantly elevated both synaptosomal GluA1 and GluA2 subunit expression relative to the UPC group in control offspring |
| GO:0045838 positive regulation of membrane potential | IMP PMID:20165912 Regulation of AMPA receptor trafficking by O-glycosylation. | MARK AS OVER ANNOTATED | Summary: Positive regulation of membrane potential (IMP), from alloxan potentiation of GluR1 currents and of hippocampal synaptic transmission. Reason: GluA1 channel opening depolarizes the postsynaptic membrane directly; that is captured by GO:1904315 (transmitter-gated channel activity involved in regulation of postsynaptic membrane potential). The cited pharmacology concerns regulation of GluA1 by O-GlcNAcylation, and a free-standing regulation-of-membrane-potential process term over-reaches. Supporting Evidence: PMID:20165912 Alloxan, an inhibitor of O-GlcNAc transferase, potentiated responses of AMPA receptors composed of the GluR1 subunit expressed in Xenopus oocytes. |
| GO:0046685 response to arsenic-containing substance | IEP PMID:19761793 Fast, quantitative in situ hybridization of rare mRNAs using... | MARK AS OVER ANNOTATED | Summary: Response to arsenic-containing substance (IEP), from a methods paper quantifying GluR1 mRNA by in situ hybridization after dimethyl arsenic acid. Reason: An mRNA-level readout in a methods demonstration; it does not show GluA1 executes a response to arsenic. Supporting Evidence: PMID:19761793 to quantify the expression of GluR1 and GluR2 subunit mRNAs of the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor in the hippocampus of untreated rats, and after intraperitoneal application of the organo-arsenic compound dimethyl arsenic acid |
| GO:0048167 regulation of synaptic plasticity | IMP PMID:12536214 PKA phosphorylation of AMPA receptor subunits controls synap... | KEEP AS NON CORE | Summary: Regulation of synaptic plasticity. Reason: Regulated insertion and removal of GluA1-containing receptors (controlled by PKA/CaMKII phosphorylation) expresses synaptic plasticity. The more specific GO:0060291 long-term synaptic potentiation (is_a descendant) is accepted in this review; this broader row is kept because the GluA1 roles also cover depression and homeostatic changes. Supporting Evidence: PMID:12536214 We found that PKA phosphorylation of the AMPA receptor subunits GluR4 and GluR1 directly controlled the synaptic incorporation of AMPA receptors in organotypic slices from rat hippocampus. PMID:15269270 The reduction in synaptic GluR1 by lithium and valproate was attributable to a reduction of surface GluR1 distribution onto the neuronal membrane |
| GO:0048167 regulation of synaptic plasticity | NAS PMID:15269270 Modulation of synaptic plasticity by antimanic agents: the r... | KEEP AS NON CORE | Summary: Regulation of synaptic plasticity. Reason: Regulated insertion and removal of GluA1-containing receptors (controlled by PKA/CaMKII phosphorylation) expresses synaptic plasticity. The more specific GO:0060291 long-term synaptic potentiation (is_a descendant) is accepted in this review; this broader row is kept because the GluA1 roles also cover depression and homeostatic changes. Supporting Evidence: PMID:12536214 We found that PKA phosphorylation of the AMPA receptor subunits GluR4 and GluR1 directly controlled the synaptic incorporation of AMPA receptors in organotypic slices from rat hippocampus. PMID:15269270 The reduction in synaptic GluR1 by lithium and valproate was attributable to a reduction of surface GluR1 distribution onto the neuronal membrane |
| GO:0048266 behavioral response to pain | IEP PMID:25716866 Persistent pain maintains morphine-seeking behavior after mo... | MARK AS OVER ANNOTATED | Summary: Behavioral response to pain (IEP): CeA GluA1 protein upregulated during morphine withdrawal in rats with persistent pain. Reason: Expression changes during a pain/morphine paradigm are readouts; the behaviour studied was morphine seeking, not a pain response executed by GluA1. Supporting Evidence: PMID:25716866 proteins of GluA1 subunits of glutamate AMPA receptors were upregulated during morphine withdrawal, and viral knockdown of CeA GluA1 eliminated the morphine-seeking behavior in withdrawn rats of the pain group |
| GO:0048787 presynaptic active zone membrane | IDA PMID:15610164 Presynaptic localization of an AMPA-type glutamate receptor ... | KEEP AS NON CORE | Summary: Presynaptic active zone membrane. Reason: Immunogold and synaptosome subfractionation detect a presynaptic GluA1 pool at active zones; minor, non-core. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0048787 presynaptic active zone membrane | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Presynaptic active zone membrane. Reason: Immunogold and synaptosome subfractionation detect a presynaptic GluA1 pool at active zones; minor, non-core. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum PMID:16903873 All of the subunits were enriched in the postsynaptic fraction but were also present in the presynaptic and non-synaptic synaptosome fractions. |
| GO:0050804 modulation of chemical synaptic transmission | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Modulation of chemical synaptic transmission. Reason: Activity-dependent delivery of GluA1-containing receptors to synapses changes synaptic strength; true, but a plasticity role secondary to the core receptor activity. Supporting Evidence: PMID:11348590 GluR1/GluR2 receptors are added to synapses during plasticity; this requires interactions between GluR1 and group I PDZ domain proteins. PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. |
| GO:0050804 modulation of chemical synaptic transmission | IDA PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | KEEP AS NON CORE | Summary: Modulation of chemical synaptic transmission. Reason: Activity-dependent delivery of GluA1-containing receptors to synapses changes synaptic strength; true, but a plasticity role secondary to the core receptor activity. Supporting Evidence: PMID:11348590 GluR1/GluR2 receptors are added to synapses during plasticity; this requires interactions between GluR1 and group I PDZ domain proteins. PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. |
| GO:0050806 positive regulation of synaptic transmission | IMP PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | KEEP AS NON CORE | Summary: Positive regulation of synaptic transmission (IMP). Reason: Delivery of GluA1/GluA2 receptors during plasticity potentiates transmission; kept as non-core alongside the accepted LTP term. Supporting Evidence: PMID:11348590 GluR1/GluR2 receptors are added to synapses during plasticity; this requires interactions between GluR1 and group I PDZ domain proteins. |
| GO:0051018 protein kinase A binding | IDA PMID:19942860 Assembly of a beta2-adrenergic receptor--GluR1 signalling co... | MARK AS OVER ANNOTATED | Summary: Protein kinase A binding (IDA), from the beta2AR-PKA-GluA1 complex. Reason: GluA1 is a PKA substrate (Ser845) and PKA is held near it by AKAP79/150 and PSD-95 in the signalling complex; the evidence shows complex membership and phosphorylation, not a direct PKA-binding activity of GluA1. Full text not available; flagged rather than removed. Supporting Evidence: PMID:19942860 Only GluR1 associated with the beta(2)AR is phosphorylated by PKA on beta(2)AR stimulation. PMID:20395454 beta(2)AR and GluR1 also form a complex comprising postsynaptic density protein 95 (PSD95), PKA and its anchor AKAP150, and protein phosphotase 2A (PP2A). |
| GO:0051428 peptide hormone receptor binding | IPI PMID:25539504 Oxytocin reduces cocaine seeking and reverses chronic cocain... | KEEP AS NON CORE | Summary: Peptide hormone receptor binding (IPI with oxytocin receptor). Reason: Reciprocal co-immunoprecipitation from rat brain shows an oxytocin receptor-GluA1 association; physiologically minor and not shown to be direct, kept as non-core. Supporting Evidence: PMID:25539504 Immunoprecipitation of oxytocin receptor and GluA1 subunit receptors further demonstrated a physical interaction between these 2 receptors |
| GO:0051602 response to electrical stimulus | IEP PMID:20554014 Involvement of microglial P2X7 receptors and downstream sign... | MARK AS OVER ANNOTATED | Summary: Response to electrical stimulus (IEP): GluR1 levels rise after sciatic-nerve tetanic stimulation or nucleus accumbens deep brain stimulation. Reason: Expression changes after electrical stimulation are readouts; they do not show that GluA1 executes a response to an electrical stimulus. Supporting Evidence: PMID:20554014 Pre-administration of the IL-1 receptor antagonist (IL-1ra) blocked both the induction of spinal LTP and the up-regulation of GluR1. |
| GO:0051602 response to electrical stimulus | IEP PMID:34742997 Deep brain stimulation of the nucleus accumbens shell attenu... | MARK AS OVER ANNOTATED | Summary: Response to electrical stimulus (IEP): GluR1 levels rise after sciatic-nerve tetanic stimulation or nucleus accumbens deep brain stimulation. Reason: Expression changes after electrical stimulation are readouts; they do not show that GluA1 executes a response to an electrical stimulus. Supporting Evidence: PMID:34742997 Finally, DBS increased both cytosolic and synaptosomal levels of GluR1, but not GluR2, in the central nucleus of the amygdala but not in other brain regions. |
| GO:0055037 recycling endosome | IEA GO_REF:0000107 | MODIFY | Summary: Recycling endosome. Reason: Correct but general for an integral membrane protein; refine to GO:0055038 recycling endosome membrane (part_of descendant), which the gene carries by IDA. Proposed replacements: recycling endosome membrane Supporting Evidence: PMID:11100149 AMPA receptors internalized in response to AMPA stimulation enter a recycling endosome system |
| GO:0055037 recycling endosome | ISO GO_REF:0000121 | MODIFY | Summary: Recycling endosome. Reason: Correct but general for an integral membrane protein; refine to GO:0055038 recycling endosome membrane (part_of descendant), which the gene carries by IDA. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P42261 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: recycling endosome membrane Supporting Evidence: PMID:11100149 AMPA receptors internalized in response to AMPA stimulation enter a recycling endosome system |
| GO:0055038 recycling endosome membrane | IDA PMID:15456832 Actin/alpha-actinin-dependent transport of AMPA receptors in... | KEEP AS NON CORE | Summary: Recycling endosome membrane. Reason: Internalized GluA1-containing receptors enter recycling endosomes before reinsertion; a trafficking location, non-core. Supporting Evidence: PMID:11100149 AMPA receptors internalized in response to AMPA stimulation enter a recycling endosome system |
| GO:0055038 recycling endosome membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Recycling endosome membrane. Reason: Internalized GluA1-containing receptors enter recycling endosomes before reinsertion; a trafficking location, non-core. Supporting Evidence: PMID:11100149 AMPA receptors internalized in response to AMPA stimulation enter a recycling endosome system |
| GO:0060076 excitatory synapse | IDA PMID:19730411 Neuroligin-1 performs neurexin-dependent and neurexin-indepe... | KEEP AS NON CORE | Summary: Excitatory synapse. Reason: True: GluA1 is at excitatory synapses. GO:0098978 glutamatergic synapse is accepted separately; the two terms are not in an is_a/part_of chain, so this row is kept as non-core. Supporting Evidence: PMID:10414981 The NMDA and AMPA classes of ionotropic glutamate receptors are concentrated at postsynaptic sites in excitatory synapses. |
| GO:0060076 excitatory synapse | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Excitatory synapse. Reason: True: GluA1 is at excitatory synapses. GO:0098978 glutamatergic synapse is accepted separately; the two terms are not in an is_a/part_of chain, so this row is kept as non-core. Supporting Evidence: PMID:10414981 The NMDA and AMPA classes of ionotropic glutamate receptors are concentrated at postsynaptic sites in excitatory synapses. |
| GO:0060078 regulation of postsynaptic membrane potential | IEA GO_REF:0000108 | ACCEPT | Summary: Regulation of postsynaptic membrane potential (IEA from GO:1904315). Reason: GluA1-containing AMPA receptors depolarize the postsynaptic membrane when glutamate binds; this is the direct physiological consequence of the core activity. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0060291 long-term synaptic potentiation | IEA GO_REF:0000117 | ACCEPT | Summary: Long-term synaptic potentiation: LTP drives GluA1-containing AMPA receptors into synapses; synaptic GluA1 rises after chemical LTP. Reason: GluA1 insertion into the postsynaptic membrane is a principal expression mechanism of NMDA receptor-dependent LTP, requiring its PDZ ligand (PMID:10731148) and transiently adding GluA2-lacking receptors (PMID:22915106). Supporting Evidence: PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP |
| GO:0060291 long-term synaptic potentiation | IEP PMID:32948689 GRIP1 regulates synaptic plasticity and learning and memory. | ACCEPT | Summary: Long-term synaptic potentiation: LTP drives GluA1-containing AMPA receptors into synapses; synaptic GluA1 rises after chemical LTP. Reason: GluA1 insertion into the postsynaptic membrane is a principal expression mechanism of NMDA receptor-dependent LTP, requiring its PDZ ligand (PMID:10731148) and transiently adding GluA2-lacking receptors (PMID:22915106). Supporting Evidence: PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. |
| GO:0060292 long-term synaptic depression | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Long-term synaptic depression (ISO from mouse Gria1). Reason: LTD is expressed by dephosphorylation and endocytosis of GluA1-containing receptors; GluA1 is the regulated cargo. Supported in rodents, kept as non-core. Supporting Evidence: PMID:11100149 insulin- and AMPA-induced AMPA receptor internalization are differentially dependent on protein phosphatases and sequence determinants within the cytoplasmic tails of GluR1 and GluR2 subunits |
| GO:0060992 response to fungicide | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Response to fungicide: long-term tributyltin exposure decreases GluR1 and GluR2 mRNA in cortical neurons. Reason: An expression change after toxicant exposure is a readout; it does not show GluA1 executes a response to fungicide. Supporting Evidence: PMID:19591855 Long-term exposure to 20 nM TBT decreased the mRNA expression of glutamate receptors NR1, NR2A, GluR1 and GluR2 |
| GO:0060992 response to fungicide | IEP PMID:19591855 Long-term exposure to endogenous levels of tributyltin decre... | MARK AS OVER ANNOTATED | Summary: Response to fungicide: long-term tributyltin exposure decreases GluR1 and GluR2 mRNA in cortical neurons. Reason: An expression change after toxicant exposure is a readout; it does not show GluA1 executes a response to fungicide. Supporting Evidence: PMID:19591855 Long-term exposure to 20 nM TBT decreased the mRNA expression of glutamate receptors NR1, NR2A, GluR1 and GluR2 |
| GO:0071230 cellular response to amino acid stimulus | IEP PMID:19913087 Early exposure of cultured hippocampal neurons to excitatory... | MARK AS OVER ANNOTATED | Summary: Cellular response to amino acid stimulus (IEP): AMPA receptor subunit expression changes after early excitatory amino acid exposure of cultured hippocampal neurons. Reason: Expression changes after excitotoxic preconditioning are readouts; GluA1 transduces glutamate as a receptor, but this row does not represent that receptor role. Supporting Evidence: PMID:19913087 Cultures were exposed to varied doses of glutamate, NMDA, or AMPA for 48 h at 5 DIV and again at 14 DIV |
| GO:0071242 cellular response to ammonium ion | ISO GO_REF:0000121 | MARK AS OVER ANNOTATED | Summary: Cellular response to ammonium ion (ISO from mouse Gria1). Reason: No rat evidence; an ammonium-induced change in AMPA receptor subunit levels or trafficking in the source species would be a readout, not a response executed by GluA1. Propagation Review Root cause: SOURCE WEAK OR INFERRED Failure modes: SOURCE EVIDENCE WEAK Sources checked: MGI:MGI:95808 SOURCE WEAK OR INFERRED Donor-side annotation reflects a readout or specialised observation that does not establish the claim for GluA1 generally. Supporting Evidence: file:rat/Gria1/Gria1-deep-research-manual.md These report changes in GluA1 protein, phosphorylation or surface level as a readout; they do not show that GluA1 executes the "response" process. |
| GO:0071345 cellular response to cytokine stimulus | IEP PMID:29112674 Interleukin-10 and PD150606 modulate expression of AMPA rece... | MARK AS OVER ANNOTATED | Summary: Cellular response to cytokine stimulus (IEP): IL-10 ameliorates the hypoxia-induced decrease in GluA1 expression. Reason: An expression readout; it does not show GluA1 executes a cytokine response. Supporting Evidence: PMID:29112674 ameliorate hypoxia-induced decrease in the expression of GluA1 and pSer831-GluA1 |
| GO:0071359 cellular response to dsRNA | IEP PMID:19958814 Glucocorticoid attenuates brain-derived neurotrophic factor-... | MARK AS OVER ANNOTATED | Summary: Cellular response to dsRNA (IEP), from transfection of a double-stranded miR-132 mimic raising GluR1 levels in cortical neurons. Reason: The "dsRNA" was a synthetic microRNA duplex used to raise miR-132 activity; GO:0071359 concerns cellular responses to double-stranded RNA as a stimulus (as in antiviral sensing). The term misrepresents the experiment, and the result is an expression readout. Supporting Evidence: PMID:19958814 Transfection of exogenous ds-miR-132 induced marked upregulation of glutamate receptors (NR2A, NR2B, and GluR1) |
| GO:0071363 cellular response to growth factor stimulus | IEP PMID:19958814 Glucocorticoid attenuates brain-derived neurotrophic factor-... | MARK AS OVER ANNOTATED | Summary: Cellular response to growth factor stimulus (IEP): BDNF-induced miR-132 upregulates GluR1 in cortical neurons. Reason: An expression readout downstream of BDNF signalling; GluA1 does not execute the growth-factor response. Supporting Evidence: PMID:19958814 Transfection of exogenous ds-miR-132 induced marked upregulation of glutamate receptors (NR2A, NR2B, and GluR1) |
| GO:0071375 cellular response to peptide hormone stimulus | IEP PMID:20237279 Leptin regulates AMPA receptor trafficking via PTEN inhibiti... | MARK AS OVER ANNOTATED | Summary: Cellular response to peptide hormone stimulus (IEP): leptin increases surface GluR1 in hippocampal slices. Reason: Surface GluA1 is the downstream target of leptin-PTEN signalling; GluA1 does not execute the hormone response. Supporting Evidence: PMID:20237279 Here we show that leptin preferentially increases the cell surface expression of GluR1 and the synaptic density of GluR2-lacking AMPA receptors in adult hippocampal slices. |
| GO:0071418 cellular response to amine stimulus | IEP PMID:19674091 Nucleus accumbens neurons exhibit synaptic scaling that is o... | MARK AS OVER ANNOTATED | Summary: Cellular response to amine stimulus (IEP): dopamine pre-exposure alters GluR1 surface expression and synaptic scaling in nucleus accumbens neurons. Reason: Surface GluA1 is the readout; GluA1 does not execute a response to amines. Supporting Evidence: PMID:19674091 Prolonged activity blockade (1-3 days) with an AMPA receptor antagonist increased cell surface (synaptic and extrasynaptic) glutamate receptor 1 (GluR1) and GluR2 but not GluR3 |
| GO:0090326 positive regulation of locomotion involved in locomotory behavior | IMP PMID:21613507 Reinforcement-related regulation of AMPA glutamate receptor ... | MARK AS OVER ANNOTATED | Summary: Positive regulation of locomotion involved in locomotory behavior (IMP): VTA GluR1 overexpression potentiated locomotor responses to intra-VTA AMPA. Reason: An overexpression gain-of-function in a drug-infusion paradigm; the behavioural readout is far downstream of GluA1 channel activity in VTA neurons and is not a GluA1-executed regulation of locomotion. Supporting Evidence: PMID:21613507 Similar GluR1(WT) overexpression potentiated locomotor responses to intra-VTA AMPA, but not NMDA, infusions. |
| GO:0097060 synaptic membrane | IDA PMID:10414981 Association of AMPA receptors with a subset of glutamate rec... | MODIFY | Summary: Synaptic membrane. Reason: Correct but general; GluA1 is mainly in the postsynaptic membrane, with a minor presynaptic pool. Refine to GO:0045211 postsynaptic membrane and GO:0042734 presynaptic membrane, is_a descendants the gene carries. Proposed replacements: postsynaptic membrane presynaptic membrane Supporting Evidence: PMID:10414981 The NMDA and AMPA classes of ionotropic glutamate receptors are concentrated at postsynaptic sites in excitatory synapses. |
| GO:0097060 synaptic membrane | IDA PMID:11910117 Control of synaptic strength by glial TNFalpha. | MODIFY | Summary: Synaptic membrane. Reason: Correct but general; GluA1 is mainly in the postsynaptic membrane, with a minor presynaptic pool. Refine to GO:0045211 postsynaptic membrane and GO:0042734 presynaptic membrane, is_a descendants the gene carries. Proposed replacements: postsynaptic membrane presynaptic membrane Supporting Evidence: PMID:11910117 enhances synaptic efficacy by increasing surface expression of AMPA receptors |
| GO:0097060 synaptic membrane | IMP PMID:27307232 Identification of PSD-95 Depalmitoylating Enzymes. | MODIFY | Summary: Synaptic membrane. Reason: Correct but general; GluA1 is mainly in the postsynaptic membrane, with a minor presynaptic pool. Refine to GO:0045211 postsynaptic membrane and GO:0042734 presynaptic membrane, is_a descendants the gene carries. Proposed replacements: postsynaptic membrane presynaptic membrane Supporting Evidence: PMID:27307232 Expression of ABHD17 in neurons selectively reduced PSD-95 palmitoylation and synaptic clustering of PSD-95 and AMPA receptors. |
| GO:0097060 synaptic membrane | ISO GO_REF:0000121 | MODIFY | Summary: Synaptic membrane. Reason: Correct but general; GluA1 is mainly in the postsynaptic membrane, with a minor presynaptic pool. Refine to GO:0045211 postsynaptic membrane and GO:0042734 presynaptic membrane, is_a descendants the gene carries. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: postsynaptic membrane presynaptic membrane Supporting Evidence: PMID:16903873 All of the subunits were enriched in the postsynaptic fraction but were also present in the presynaptic and non-synaptic synaptosome fractions. |
| GO:0097110 scaffold protein binding | IPI PMID:10939335 Targeting of PKA to glutamate receptors through a MAGUK-AKAP... | KEEP AS NON CORE | Summary: Scaffold protein binding: GluA1 associates with SAP97 (and via SAP97 with AKAP79/150). Reason: GluA1 binds the scaffold SAP97 through its C-terminal PDZ ligand; BDNF increases GluR1-SAP97 association. True but the specific activity is captured by PDZ domain binding (core); the AKAP79 row reflects a MAGUK-AKAP ternary complex in which SAP97 bridges GluA1 and the AKAP. Supporting Evidence: PMID:10939335 Two classes of binding proteins organize these complexes: the MAGUK proteins that cluster glutamate receptors and AKAPs that anchor kinases and phosphatases. |
| GO:0097110 scaffold protein binding | IPI PMID:14597197 Brain-derived neurotrophic factor signal enhances and mainta... | KEEP AS NON CORE | Summary: Scaffold protein binding: GluA1 associates with SAP97 (and via SAP97 with AKAP79/150). Reason: GluA1 binds the scaffold SAP97 through its C-terminal PDZ ligand; BDNF increases GluR1-SAP97 association. True but the specific activity is captured by PDZ domain binding (core); the AKAP79 row reflects a MAGUK-AKAP ternary complex in which SAP97 bridges GluA1 and the AKAP. Supporting Evidence: PMID:14597197 The BDNF-triggered increases in PDZ proteins resulted in the elevation of their total association with the AMPA receptors GluR1 and GluR2/3, which led to the increase in AMPA receptor proteins. |
| GO:0097110 scaffold protein binding | IPI PMID:23460828 Acute BDNF treatment upregulates GluR1-SAP97 and GluR2-GRIP1... | KEEP AS NON CORE | Summary: Scaffold protein binding: GluA1 associates with SAP97 (and via SAP97 with AKAP79/150). Reason: GluA1 binds the scaffold SAP97 through its C-terminal PDZ ligand; BDNF increases GluR1-SAP97 association. True but the specific activity is captured by PDZ domain binding (core); the AKAP79 row reflects a MAGUK-AKAP ternary complex in which SAP97 bridges GluA1 and the AKAP. Supporting Evidence: PMID:23460828 Our results show that acute BDNF treatment upregulates the interactions between AMPAr subunits (GluR1 and GluR2) with their scaffold proteins SAP97 and GRIP1, respectively |
| GO:0098685 Schaffer collateral - CA1 synapse | NAS PMID:30872532 Architecture of the heteromeric GluA1/2 AMPA receptor in com... | KEEP AS NON CORE | Summary: Schaffer collateral - CA1 synapse (NAS). Reason: GluA1/GluA2-TARP gamma-8 receptors are the principal AMPAR complex at hippocampal (including Schaffer collateral-CA1) synapses; a specific anatomical synapse type, non-core. Supporting Evidence: PMID:30872532 Here, we present a cryo-electron microscopy structure of the heteromeric GluA1/2 receptor associated with two transmembrane AMPAR regulatory protein (TARP) Ξ³8 auxiliary subunits, the principal AMPAR complex at hippocampal synapses. |
| GO:0098793 presynapse | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Presynapse. Reason: A minor presynaptic GluA1 pool is supported by immunogold and synaptosome subfractionation; non-core. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0098793 presynapse | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Presynapse. Reason: A minor presynaptic GluA1 pool is supported by immunogold and synaptosome subfractionation; non-core. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0098793 presynapse | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Presynapse. Reason: A minor presynaptic GluA1 pool is supported by immunogold and synaptosome subfractionation; non-core. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0098794 postsynapse | ISO GO_REF:0000121 | MODIFY | Summary: Postsynapse (ISO from mouse). Reason: Correct but general; GluA1 is in the postsynaptic density membrane (GO:0098839, part_of descendant), which the gene carries by IBA, IDA and ISO. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95808 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0098839 postsynaptic density membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Postsynaptic density membrane. Reason: Core location: GluA1-containing AMPA receptors are anchored in the PSD membrane of glutamatergic synapses and their PSD content rises with LTP. Supporting Evidence: PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0098839 postsynaptic density membrane | IDA PMID:15610164 Presynaptic localization of an AMPA-type glutamate receptor ... | ACCEPT | Summary: Postsynaptic density membrane. Reason: Core location: GluA1-containing AMPA receptors are anchored in the PSD membrane of glutamatergic synapses and their PSD content rises with LTP. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0098839 postsynaptic density membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Postsynaptic density membrane. Reason: Core location: GluA1-containing AMPA receptors are anchored in the PSD membrane of glutamatergic synapses and their PSD content rises with LTP. Supporting Evidence: PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0098839 postsynaptic density membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic density membrane. Reason: Core location: GluA1-containing AMPA receptors are anchored in the PSD membrane of glutamatergic synapses and their PSD content rises with LTP. Supporting Evidence: PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0098839 postsynaptic density membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic density membrane. Reason: Core location: GluA1-containing AMPA receptors are anchored in the PSD membrane of glutamatergic synapses and their PSD content rises with LTP. Supporting Evidence: PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0098839 postsynaptic density membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Postsynaptic density membrane. Reason: Core location: GluA1-containing AMPA receptors are anchored in the PSD membrane of glutamatergic synapses and their PSD content rises with LTP. Supporting Evidence: PMID:32948689 we saw significant increases in synaptic GluA1, GluA2, and GluA3 AMPAR subunits after cLTP PMID:21425350 Brief intake of sucrose increased GluR1 in the PSD, regardless of dietary condition, though the net effect was greater in FR than AL subjects. |
| GO:0098978 glutamatergic synapse | IDA PMID:10731148 Driving AMPA receptors into synapses by LTP and CaMKII: requ... | ACCEPT | Summary: Glutamatergic synapse. Reason: Core location: GluA1 is a subunit of the AMPA receptors that mediate glutamatergic transmission; LTP drives GluA1 receptors into these synapses. Supporting Evidence: PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. |
| GO:0098978 glutamatergic synapse | IDA PMID:15610164 Presynaptic localization of an AMPA-type glutamate receptor ... | ACCEPT | Summary: Glutamatergic synapse. Reason: Core location: GluA1 is a subunit of the AMPA receptors that mediate glutamatergic transmission; LTP drives GluA1 receptors into these synapses. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000117 | ACCEPT | Summary: Glutamatergic synapse. Reason: Core location: GluA1 is a subunit of the AMPA receptors that mediate glutamatergic transmission; LTP drives GluA1 receptors into these synapses. Supporting Evidence: PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0098978 glutamatergic synapse | IMP PMID:10731148 Driving AMPA receptors into synapses by LTP and CaMKII: requ... | ACCEPT | Summary: Glutamatergic synapse. Reason: Core location: GluA1 is a subunit of the AMPA receptors that mediate glutamatergic transmission; LTP drives GluA1 receptors into these synapses. Supporting Evidence: PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. |
| GO:0098978 glutamatergic synapse | ISO GO_REF:0000121 | ACCEPT | Summary: Glutamatergic synapse. Reason: Core location: GluA1 is a subunit of the AMPA receptors that mediate glutamatergic transmission; LTP drives GluA1 receptors into these synapses. Supporting Evidence: PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0098978 glutamatergic synapse | ISO GO_REF:0000121 | ACCEPT | Summary: Glutamatergic synapse. Reason: Core location: GluA1 is a subunit of the AMPA receptors that mediate glutamatergic transmission; LTP drives GluA1 receptors into these synapses. Supporting Evidence: PMID:10731148 These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein. PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0099092 postsynaptic density, intracellular component | IDA PMID:26088419 Activity-induced synaptic delivery of the GluN2A-containing ... | UNDECIDED | Summary: Postsynaptic density, intracellular component (IDA), from a study of Bip-dependent synaptic delivery of GluN2A-containing NMDA receptors. Reason: The cached abstract concerns GluN2A and does not mention GluA1; full text not available. GluA1 is an integral membrane protein whose cytoplasmic tail faces the PSD, so the membrane term (GO:0098839) is the expected location; whether the curator saw GluA1 specifically in a PSD intracellular fraction cannot be checked. Supporting Evidence: PMID:26088419 Bip, an endoplasmic reticulum (ER) chaperone, selectively interacted with GluN2A and mediated the neuronal activity-induced assembly and synaptic incorporation of the GluN2A-containing NMDAR from dendritic ER |
| GO:0099505 regulation of presynaptic membrane potential | IEA GO_REF:0000108 | MARK AS OVER ANNOTATED | Summary: Regulation of presynaptic membrane potential (IEA, inferred from GO:0099507). Reason: Inherited from the presynaptic channel-activity term, which this review generalises; there is no rat evidence that presynaptic GluA1-containing receptors regulate presynaptic membrane potential. Supporting Evidence: PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0099507 ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential | IEA GO_REF:0000107 | MODIFY | Summary: Ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential. Reason: GluA1 does have ligand-gated cation channel activity and a minor presynaptic pool exists, but no evidence reviewed here shows presynaptic GluA1 receptors regulating presynaptic membrane potential. Generalise to the activity, GO:0004971 AMPA glutamate receptor activity, and drop the presynaptic context. Proposed replacements: AMPA glutamate receptor activity Context of precomposed term: context dropped Presynaptic membrane-potential context is unsupported for GluA1 (over-annotation of the context). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0099507 ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential | ISO GO_REF:0000121 | MODIFY | Summary: Ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential. Reason: GluA1 does have ligand-gated cation channel activity and a minor presynaptic pool exists, but no evidence reviewed here shows presynaptic GluA1 receptors regulating presynaptic membrane potential. Generalise to the activity, GO:0004971 AMPA glutamate receptor activity, and drop the presynaptic context. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P42261 SUPPORTS TRANSFER Same AMPA-receptor subunit ortholog; the claim transfers and only the term granularity is refined. Proposed replacements: AMPA glutamate receptor activity Context of precomposed term: context dropped Presynaptic membrane-potential context is unsupported for GluA1 (over-annotation of the context). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:15610164 Immunoreactive gold particles for AMPA receptor subunits GluR1 and GluR2/3 were frequently found not only on postsynaptic but also on presynaptic profiles immunopositive for VGluT1 and VGluT2 in the neostriatum |
| GO:0099544 perisynaptic space | ISO GO_REF:0000121 | MARK AS OVER ANNOTATED | Summary: Perisynaptic space (ISO from mouse Gria1). Reason: GO:0099544 is defined as the extracellular region adjacent to a synapse. GluA1 is an integral membrane protein; perisynaptic (extrasynaptic) receptors sit in the plasma membrane, not in the extracellular space, so the term misplaces the protein. Propagation Review Root cause: SOURCE WEAK OR INFERRED Failure modes: SOURCE EVIDENCE WEAK Sources checked: MGI:MGI:95808 SOURCE WEAK OR INFERRED Donor-side annotation reflects a readout or specialised observation that does not establish the claim for GluA1 generally. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid |
| GO:0099604 ligand-gated calcium channel activity | IDA PMID:1709304 Ca2+ permeability of KA-AMPA--gated glutamate receptor chann... | MODIFY | Summary: Ligand-gated calcium channel activity (IDA): KA- and AMPA-evoked Ca2+ currents through GluR1 receptors. Reason: Correct but less specific: the ligand is glutamate. Refine to GO:0022849 glutamate-gated calcium ion channel activity, an is_a descendant the gene carries by IDA. Proposed replacements: glutamate-gated calcium ion channel activity Supporting Evidence: PMID:1709304 At physiological resting potentials, KA and AMPA elicited inward calcium currents in oocytes expressing GluR1, GluR3, and GluR1 plus GluR3. |
| GO:1904315 transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | IBA GO_REF:0000033 | ACCEPT | Summary: Transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential. Reason: Core activity: GluA1-containing AMPA receptors are glutamate-gated cation channels that depolarize the postsynaptic membrane at glutamatergic synapses; synaptic delivery of tagged GluA1 changes postsynaptic currents (PMID:10731148). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. |
| GO:1904315 transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | IDA PMID:10731148 Driving AMPA receptors into synapses by LTP and CaMKII: requ... | ACCEPT | Summary: Transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential. Reason: Core activity: GluA1-containing AMPA receptors are glutamate-gated cation channels that depolarize the postsynaptic membrane at glutamatergic synapses; synaptic delivery of tagged GluA1 changes postsynaptic currents (PMID:10731148). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. |
| GO:1904315 transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | IMP PMID:10731148 Driving AMPA receptors into synapses by LTP and CaMKII: requ... | ACCEPT | Summary: Transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential. Reason: Core activity: GluA1-containing AMPA receptors are glutamate-gated cation channels that depolarize the postsynaptic membrane at glutamatergic synapses; synaptic delivery of tagged GluA1 changes postsynaptic currents (PMID:10731148). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. |
| GO:1904315 transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | ISO GO_REF:0000121 | ACCEPT | Summary: Transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential. Reason: Core activity: GluA1-containing AMPA receptors are glutamate-gated cation channels that depolarize the postsynaptic membrane at glutamatergic synapses; synaptic delivery of tagged GluA1 changes postsynaptic currents (PMID:10731148). Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:10731148 Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. |
| GO:1905232 cellular response to L-glutamate | IEP PMID:12390532 D1 dopamine receptor stimulation increases GluR1 surface exp... | KEEP AS NON CORE | Summary: Cellular response to L-glutamate (IEP), from a study of GluR1 surface expression in nucleus accumbens neurons. Reason: GluA1 is itself a glutamate receptor, so it does participate in the cellular response to L-glutamate as the sensor and channel; the row is kept, as non-core, because the specific receptor role is captured by AMPA glutamate receptor activity and the IEP readout here is surface expression. Supporting Evidence: file:rat/Gria1/Gria1-uniprot.txt Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid PMID:12390532 Regulation of the surface expression of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor subunit GluR1 plays a critical role in long-term potentiation |
| GO:1905430 cellular response to glycine | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Cellular response to glycine: glycine (chemical LTP) induces synaptic insertion of GluA1. Reason: Glycine is used as a chemical-LTP stimulus that co-activates NMDA receptors; GluA1 insertion is the downstream plasticity readout, captured by LTP, not a glycine response executed by GluA1. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. PMID:32948689 Cultured rat cortical neurons were treated with glycine to induce chemically mediated LTP (cLTP) |
| GO:1905430 cellular response to glycine | IEP PMID:22915106 PICK1 mediates transient synaptic expression of GluA2-lackin... | MARK AS OVER ANNOTATED | Summary: Cellular response to glycine: glycine (chemical LTP) induces synaptic insertion of GluA1. Reason: Glycine is used as a chemical-LTP stimulus that co-activates NMDA receptors; GluA1 insertion is the downstream plasticity readout, captured by LTP, not a glycine response executed by GluA1. Supporting Evidence: PMID:22915106 Here, we show that endogenous GluA1 is rapidly inserted at the synaptic plasma membrane of rat hippocampal neurons immediately after stimulation with elevated glycine, a treatment known to induce LTP. |
| GO:1905430 cellular response to glycine | IEP PMID:32948689 GRIP1 regulates synaptic plasticity and learning and memory. | MARK AS OVER ANNOTATED | Summary: Cellular response to glycine: glycine (chemical LTP) induces synaptic insertion of GluA1. Reason: Glycine is used as a chemical-LTP stimulus that co-activates NMDA receptors; GluA1 insertion is the downstream plasticity readout, captured by LTP, not a glycine response executed by GluA1. Supporting Evidence: PMID:32948689 Cultured rat cortical neurons were treated with glycine to induce chemically mediated LTP (cLTP) |
| GO:1990416 cellular response to brain-derived neurotrophic factor stimulus | IDA PMID:14597197 Brain-derived neurotrophic factor signal enhances and mainta... | MARK AS OVER ANNOTATED | Summary: Cellular response to BDNF stimulus: BDNF increases GluR1 protein, surface level and association with SAP97. Reason: GluA1 is a downstream target of BDNF-TrkB signalling; changes in its level and trafficking are readouts, not a BDNF response executed by GluA1. Supporting Evidence: PMID:14597197 The BDNF-triggered increases in PDZ proteins resulted in the elevation of their total association with the AMPA receptors GluR1 and GluR2/3, which led to the increase in AMPA receptor proteins. |
| GO:1990416 cellular response to brain-derived neurotrophic factor stimulus | IDA PMID:23460828 Acute BDNF treatment upregulates GluR1-SAP97 and GluR2-GRIP1... | MARK AS OVER ANNOTATED | Summary: Cellular response to BDNF stimulus: BDNF increases GluR1 protein, surface level and association with SAP97. Reason: GluA1 is a downstream target of BDNF-TrkB signalling; changes in its level and trafficking are readouts, not a BDNF response executed by GluA1. Supporting Evidence: PMID:23460828 Our results show that acute BDNF treatment upregulates the interactions between AMPAr subunits (GluR1 and GluR2) with their scaffold proteins SAP97 and GRIP1, respectively |
| GO:1990416 cellular response to brain-derived neurotrophic factor stimulus | IEP PMID:24712995 BDNF contributes to both rapid and homeostatic alterations i... | MARK AS OVER ANNOTATED | Summary: Cellular response to BDNF stimulus: BDNF increases GluR1 protein, surface level and association with SAP97. Reason: GluA1 is a downstream target of BDNF-TrkB signalling; changes in its level and trafficking are readouts, not a BDNF response executed by GluA1. Supporting Evidence: PMID:24712995 Immunocytochemical studies showed that acute BDNF treatment increased cell surface GluA1 and GluA2 levels, as well as their co-localization, on NAc neurons. |
| GO:1990635 proximal dendrite | IDA PMID:23844251 Soluble ICAM-5, a product of activity dependent proteolysis,... | KEEP AS NON CORE | Summary: Proximal dendrite (IDA): soluble ICAM-5 increases GluA1 in dendrites. Reason: A real dendritic location, less informative than the PSD membrane; non-core. Supporting Evidence: PMID:23844251 the ICAM-5 ectodomain stimulates an increase in membrane levels of GluA1, but not GluA2, AMPAR subunits |
| GO:1990708 conditioned place preference | IMP PMID:23345231 Central amygdala GluA1 facilitates associative learning of o... | KEEP AS NON CORE | Summary: Conditioned place preference (IMP): CeA GluA1 knockdown inhibits morphine CPP acquisition and extinction; overexpression accelerates them. Reason: Bidirectional manipulation supports a requirement of CeA GluA1-containing receptors for this associative learning; a behavioural, non-core role downstream of synaptic plasticity. Supporting Evidence: PMID:23345231 Adenoviral shRNA-mediated downregulation of CeA GluA1 produced opposite effects, inhibiting the processes of both CPP acquisition and CPP extinction. |
| GO:1990911 response to psychosocial stress | IEP PMID:32594591 Enhanced psychostimulant response, but not social avoidance,... | MARK AS OVER ANNOTATED | Summary: Response to psychosocial stress (IEP): intermittent social defeat stress induces GluA1 expression in VTA dopamine neurons. Reason: Increased GluA1 expression is the stress-induced readout; inactivating VTA GluA1 AMPARs blocked amphetamine cross-sensitization but not social avoidance, so the paper itself does not support GluA1 executing the stress response. Supporting Evidence: PMID:32594591 Social defeat stress exposure induced GluA1 expression in VTA DA neurons |
| GO:2000463 positive regulation of excitatory postsynaptic potential | IMP PMID:23345231 Central amygdala GluA1 facilitates associative learning of o... | KEEP AS NON CORE | Summary: Positive regulation of excitatory postsynaptic potential (IMP): GluA1 overexpression enhances postsynaptic GluA2-lacking AMPA receptor responses in CeA neurons. Reason: GluA1 carries the excitatory postsynaptic current; increasing GluA1 increases EPSPs. True, but secondary to the core activity. Supporting Evidence: PMID:23345231 Whole-cell recording revealed enhanced electrophysiological properties of postsynaptic GluA2-lacking AMPA receptors in adenoviral GluA1-infected CeA neurons. |
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Download this section (compressed HTML)Q: Should RGD and SynGO rows that place GluA1 at cellular components with IEP or IMP evidence (presynaptic membrane, postsynaptic membrane, glutamatergic synapse, synapse, synaptic membrane) be re-coded as IDA where the papers localise GluA1 directly?
Q: Do presynaptic GluA1-containing AMPA receptors in corticostriatal and thalamostriatal terminals regulate presynaptic membrane potential or glutamate release, which would be needed to justify GO:0099507 for GluA1?
Q: Is the beta2-adrenergic receptor/Gs/adenylyl cyclase/PKA association with GluA1 direct for any component, or entirely bridged by stargazin, PSD-95 and AKAP150, which would make the G-protein, adenylate cyclase and PKA binding rows complex-membership statements?
Experiment: Use terminal-specific Gria1 deletion (cortical or thalamic Cre lines) and measure paired-pulse ratio, presynaptic Ca2+ imaging and terminal membrane potential at corticostriatal and thalamostriatal synapses after AMPA application.
Hypothesis: Presynaptic GluA1-containing AMPA receptors depolarize striatal glutamatergic terminals and modulate release.
Experiment: Reconstitute beta2AR, Gs, adenylyl cyclase and GluA1 in heterologous cells with or without stargazin, PSD-95 and AKAP150, and test pairwise binding by co-immunoprecipitation and proximity labelling, alongside in vitro binding with purified GluA1 C-tail.
Hypothesis: Gs, adenylyl cyclase and PKA reach GluA1 only through stargazin/PSD-95/AKAP150 scaffolds.
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