Gria2 encodes GluA2 (GluR2, GluR-B), a pore-forming subunit of AMPA-type ionotropic glutamate receptors. GluA2 assembles with GluA1, GluA3 or GluA4 (or as homomers) into tetrameric glutamate-gated cation channels, together with auxiliary TARP and cornichon subunits, and these receptors mediate most fast excitatory transmission at glutamatergic synapses, where they are anchored in the postsynaptic density membrane of dendritic spines. GluA2 dominates the properties of heteromeric receptors: RNA editing of the pore-loop Q/R site (Gln607Arg) makes GluA2-containing receptors Ca2+-impermeable and shapes rectification, and flip/flop splicing tunes desensitization. The cytoplasmic C-terminal tail is a trafficking hub: its PDZ ligand binds GRIP1/ABP and PICK1, a membrane-proximal motif binds NSF, and a basic motif binds AP-2, so that phosphorylation-regulated interactions control synaptic delivery, clustering, recycling and the endocytosis that expresses long-term depression and homeostatic scaling. Smaller GluA2 pools occur in presynaptic terminals and synaptic vesicle membranes.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000149 SNARE binding | IPI PMID:11931741 NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA recept... | MARK AS OVER ANNOTATED | Summary: SNARE binding, from the GluR2-PICK1-NSF-SNAP complex study; the With partner is PICK1. Reason: PICK1, NSF and alpha/beta-SNAP are not SNARE proteins; the abstract itself describes the GluR2-PICK1 complex as a non-SNARE substrate for NSF. The interaction is real but the SNARE binding term does not describe it. Full text not available, so the row is flagged rather than removed. Supporting Evidence: PMID:11931741 Furthermore, we are reporting a non-SNARE substrate for NSF disassembly activity. PMID:11931741 Here, we show that GluR2, PICK1, NSF, and alpha-/beta-SNAPs form a complex in the presence of ATPgammaS. |
| GO:0001540 amyloid-beta binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Amyloid-beta binding (IEA); soluble Abeta oligomers (ADDLs) associate preferentially with GluA2-containing AMPA receptor complexes on dendritic spines. Reason: Supported by co-immunoprecipitation and photo-crosslinking in hippocampal neurons (PMID:20032460). This is a pathological ligand interaction relevant to Alzheimer disease models, not part of the physiological function of GluA2, so it is kept as non-core. Supporting Evidence: PMID:20032460 we found that ADDLs interact preferentially with GluR2-containing complexes. |
| GO:0001540 amyloid-beta binding | IPI PMID:20032460 Inhibition of calcineurin-mediated endocytosis and alpha-ami... | KEEP AS NON CORE | Summary: Amyloid-beta binding (IPI); soluble Abeta oligomers (ADDLs) associate preferentially with GluA2-containing AMPA receptor complexes on dendritic spines. Reason: Supported by co-immunoprecipitation and photo-crosslinking in hippocampal neurons (PMID:20032460). This is a pathological ligand interaction relevant to Alzheimer disease models, not part of the physiological function of GluA2, so it is kept as non-core. Supporting Evidence: PMID:20032460 we found that ADDLs interact preferentially with GluR2-containing complexes. |
| GO:0001919 regulation of receptor recycling | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Regulation of receptor recycling (IEA), based on GluR2/3 receptors continuously replacing synaptic receptors in an NSF- and PDZ-dependent manner. Reason: GluA2 is the receptor that recycles (the cargo); its C-tail motifs recruit NSF and PDZ proteins, which do the regulating. The GluA2 C-tail is needed for its own recycling, but that is not the gene product regulating receptor recycling as a process. Core trafficking role is captured by PDZ domain binding. Supporting Evidence: PMID:11348590 GluR2/GluR3 receptors replace existing synaptic receptors continuously; this occurs only at synapses that already have AMPA-Rs and requires interactions by GluR2 with NSF and group II PDZ domain proteins. PMID:16037816 NEEP21-GRIP1 binding is crucial for GluR2-AMPAR sorting through endosomes and their recruitment to the plasma membrane |
| 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 (IMP), based on GluR2/3 receptors continuously replacing synaptic receptors in an NSF- and PDZ-dependent manner. Reason: GluA2 is the receptor that recycles (the cargo); its C-tail motifs recruit NSF and PDZ proteins, which do the regulating. The GluA2 C-tail is needed for its own recycling, but that is not the gene product regulating receptor recycling as a process. Core trafficking role is captured by PDZ domain binding. Supporting Evidence: PMID:11348590 GluR2/GluR3 receptors replace existing synaptic receptors continuously; this occurs only at synapses that already have AMPA-Rs and requires interactions by GluR2 with NSF and group II PDZ domain proteins. PMID:16037816 NEEP21-GRIP1 binding is crucial for GluR2-AMPAR sorting through endosomes and their recruitment to the plasma membrane |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:19946266 X-ray structure, symmetry and mechanism of an AMPA-subtype g... | MODIFY | Summary: Glutamate-gated receptor activity (IDA); GluA2 is an AMPA-type ionotropic glutamate receptor subunit. Reason: Correct but less specific than the evidence: GluA2 is an AMPA-type receptor subunit (crystal structure of the AMPA-sensitive GluA2 tetramer; AMPA > glutamate > kainate pharmacology). Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. file:rat/Gria2/Gria2-uniprot.txt This receptor binds AMPA (quisqualate) > L-glutamate > kainate |
| GO:0004970 glutamate-gated receptor activity | IDA PMID:21846932 Mechanism of AMPA receptor activation by partial agonists: d... | MODIFY | Summary: Glutamate-gated receptor activity (IDA); GluA2 is an AMPA-type ionotropic glutamate receptor subunit. Reason: Correct but less specific than the evidence: GluA2 is an AMPA-type receptor subunit (crystal structure of the AMPA-sensitive GluA2 tetramer; AMPA > glutamate > kainate pharmacology). Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. file:rat/Gria2/Gria2-uniprot.txt This receptor binds AMPA (quisqualate) > L-glutamate > kainate |
| GO:0004970 glutamate-gated receptor activity | ISO GO_REF:0000121 | MODIFY | Summary: Glutamate-gated receptor activity (ISO from the mouse/human GluA2 ortholog). Reason: Transfer from the GluA2 ortholog is sound; the term is less specific than warranted. Refine to GO:0004971 AMPA glutamate receptor activity, 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:95809 SUPPORTS TRANSFER Ortholog of the same AMPA subunit; only term granularity is refined. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. file:rat/Gria2/Gria2-uniprot.txt This receptor binds AMPA (quisqualate) > L-glutamate > kainate |
| GO:0004970 glutamate-gated receptor activity | ISO GO_REF:0000121 | MODIFY | Summary: Glutamate-gated receptor activity (ISO from the mouse/human GluA2 ortholog). Reason: Transfer from the GluA2 ortholog is sound; the term is less specific than warranted. Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant the gene carries by IBA and IDA. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P42262 SUPPORTS TRANSFER Ortholog of the same AMPA subunit; only term granularity is refined. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. file:rat/Gria2/Gria2-uniprot.txt This receptor binds AMPA (quisqualate) > L-glutamate > kainate |
| GO:0004970 glutamate-gated receptor activity | TAS PMID:12554656 Regulated delivery of AMPA receptor subunits to the presynap... | MODIFY | Summary: Glutamate-gated receptor activity (TAS); GluA2 is an AMPA-type ionotropic glutamate receptor subunit. Reason: Correct but less specific than the evidence: GluA2 is an AMPA-type receptor subunit (crystal structure of the AMPA-sensitive GluA2 tetramer; AMPA > glutamate > kainate pharmacology). Refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant that the gene already carries by IBA and IDA. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. file:rat/Gria2/Gria2-uniprot.txt This receptor binds AMPA (quisqualate) > L-glutamate > kainate |
| GO:0004971 AMPA glutamate receptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: AMPA glutamate receptor activity (IBA). GluA2 is a pore-forming, glutamate-binding subunit of AMPA receptors. Reason: Core function. GluA2 binds glutamate in its S1/S2 domain and forms the cation pore of homo- and heteromeric AMPA receptors; it dominates gating in GluA1/2 heteromers and its edited Q/R site sets Ca2+ impermeability. Native AMPARs containing GluA2 with TARP and cornichon auxiliary subunits show this activity. Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. PMID:30872532 Within the receptor, the core subunits arrange to give the GluA2 subunit dominant control of gating. |
| GO:0004971 AMPA glutamate receptor activity | IDA PMID:19265014 Functional proteomics identify cornichon proteins as auxilia... | ACCEPT | Summary: AMPA glutamate receptor activity (IDA). GluA2 is a pore-forming, glutamate-binding subunit of AMPA receptors. Reason: Core function. GluA2 binds glutamate in its S1/S2 domain and forms the cation pore of homo- and heteromeric AMPA receptors; it dominates gating in GluA1/2 heteromers and its edited Q/R site sets Ca2+ impermeability. Native AMPARs containing GluA2 with TARP and cornichon auxiliary subunits show this activity. 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:0004971 AMPA glutamate receptor activity | IDA PMID:21172611 Hippocampal AMPA receptor gating controlled by both TARP and... | ACCEPT | Summary: AMPA glutamate receptor activity (IDA). GluA2 is a pore-forming, glutamate-binding subunit of AMPA receptors. Reason: Core function. GluA2 binds glutamate in its S1/S2 domain and forms the cation pore of homo- and heteromeric AMPA receptors; it dominates gating in GluA1/2 heteromers and its edited Q/R site sets Ca2+ impermeability. Native AMPARs containing GluA2 with TARP and cornichon auxiliary subunits show this activity. Supporting Evidence: PMID:21172611 Thus, Ξ³-8 and CNIH-2 functionally interact with common hippocampal AMPA receptor complexes to modulate synergistically kinetics and pharmacology. |
| GO:0004971 AMPA glutamate receptor activity | IEA GO_REF:0000117 | ACCEPT | Summary: AMPA glutamate receptor activity (IEA). GluA2 is a pore-forming, glutamate-binding subunit of AMPA receptors. Reason: Core function. GluA2 binds glutamate in its S1/S2 domain and forms the cation pore of homo- and heteromeric AMPA receptors; it dominates gating in GluA1/2 heteromers and its edited Q/R site sets Ca2+ impermeability. Native AMPARs containing GluA2 with TARP and cornichon auxiliary subunits show this activity. Supporting Evidence: file:rat/Gria2/Gria2-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 | TAS PMID:12554656 Regulated delivery of AMPA receptor subunits to the presynap... | ACCEPT | Summary: AMPA glutamate receptor activity (TAS). GluA2 is a pore-forming, glutamate-binding subunit of AMPA receptors. Reason: Core function. GluA2 binds glutamate in its S1/S2 domain and forms the cation pore of homo- and heteromeric AMPA receptors; it dominates gating in GluA1/2 heteromers and its edited Q/R site sets Ca2+ impermeability. Native AMPARs containing GluA2 with TARP and cornichon auxiliary subunits show this activity. Supporting Evidence: PMID:12554656 We demonstrate that the AMPA receptor subunits GluR1 and GluR2 are expressed and organized in functional receptors in axonal growth cones of hippocampal neurons. |
| GO:0005216 monoatomic ion channel activity | IEA GO_REF:0000002 | MODIFY | Summary: Monoatomic ion channel activity (IEA, InterPro). Reason: Correct but too general; refine to GO:0004971 AMPA glutamate receptor activity (an is_a descendant the gene already carries). Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: file:rat/Gria2/Gria2-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:0005230 extracellular ligand-gated monoatomic ion channel activity | IDA PMID:1653450 Identification of a site in glutamate receptor subunits that... | MODIFY | Summary: Extracellular ligand-gated monoatomic ion channel activity (IDA), from the Q/R site study of non-NMDA receptor permeation. Reason: Correct, but GluA2 is specifically an AMPA receptor subunit; refine to GO:0004971 AMPA glutamate receptor activity, an is_a descendant the gene carries. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:1653450 Mutation of a certain amino acid that results in a net charge change (from glutamine to arginine or vice versa) alters both the current-voltage relation and the calcium permeability of non-NMDA receptors. |
| GO:0005234 extracellularly glutamate-gated ion channel activity | ISO GO_REF:0000121 | ACCEPT | Summary: Extracellularly glutamate-gated ion channel activity (ISO from mouse Gria2). Reason: True: the GluA2-containing channel opens when glutamate binds the extracellular ligand-binding domain. This term sits in a parallel branch to GO:0004971 (not an ancestor), so it is kept as is alongside the AMPA receptor term. Supporting Evidence: PMID:19946266 function by opening a transmembrane ion channel upon binding of glutamate file:rat/Gria2/Gria2-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:10027300 Clustering of AMPA receptors by the synaptic PDZ domain-cont... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:10340301 The protein kinase C alpha binding protein PICK1 interacts w... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:10558890 rDLG6: a novel homolog of Drosophila DLG expressed in rat br... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:11891216 The PDZ proteins PICK1, GRIP, and syntenin bind multiple glu... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:11891216 The PDZ proteins PICK1, GRIP, and syntenin bind multiple glu... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:11931740 Interaction between GRIP and liprin-alpha/SYD2 is required f... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:11931740 Interaction between GRIP and liprin-alpha/SYD2 is required f... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:11931740 Interaction between GRIP and liprin-alpha/SYD2 is required f... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:12130635 Brain-derived neurotrophic factor regulates surface expressi... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:16037816 Interactions between NEEP21, GRIP1 and GluR2 regulate sortin... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:16037816 Interactions between NEEP21, GRIP1 and GluR2 regulate sortin... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both 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). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. This row cites PMID:16108831, a paper on IGSF11 as a cancer-vaccine target that contains no GluA2 data; the intended reference is probably PMID:26595655 (IgSF11 binds AMPARs). |
| GO:0005515 protein binding | IPI PMID:16338934 Involvement of myosin Vb in glutamate receptor trafficking. | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:17289840 Molecular determinants for the interaction between AMPA rece... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:17914463 Clustering and synaptic targeting of PICK1 requires direct i... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both 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). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both 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). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both 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). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:20018661 Identification of a small-molecule inhibitor of the PICK1 PD... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both 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). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both 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). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:21496646 The AAA+ ATPase Thorase regulates AMPA receptor-dependent sy... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:21496646 The AAA+ ATPase Thorase regulates AMPA receptor-dependent sy... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:21847098 PIKE-mediated PI3-kinase activity is required for AMPA recep... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:21847098 PIKE-mediated PI3-kinase activity is required for AMPA recep... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both 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). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:27756895 MPP2 is a postsynaptic MAGUK scaffold protein that links Syn... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:30545844 Synaptotagmin-3 drives AMPA receptor endocytosis, depression... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:9647694 CIPP, a novel multivalent PDZ domain protein, selectively in... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:9697854 NSF binding to GluR2 regulates synaptic transmission. | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:9768844 Novel anchorage of GluR2/3 to the postsynaptic density by th... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005515 protein binding | IPI PMID:9768844 Novel anchorage of GluR2/3 to the postsynaptic density by th... | REMOVE | Summary: Bare protein binding (IPI). GluA2 interacts with many trafficking partners (PICK1, GRIP1/2, NSF, AP-2, TARPs, liprins, PIKE, Thorase, Syt3, GluA1). 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 activity behind most of these rows is PDZ domain binding by the GluA2 C-terminus or AMPA receptor complex assembly, both captured elsewhere in this review. |
| GO:0005783 endoplasmic reticulum | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Endoplasmic reticulum (ISO from mouse Gria2). Reason: Root organelle term from an ISO transfer; the claim holds: GluA2 is synthesised and assembled in the ER and edited (R) GluA2 has a substantial ER-resident pool, and assembly via the ATD occurs there. It is a biosynthetic location, not where the channel functions, so non-core. Supporting Evidence: PMID:21317873 Heteromerization is dominant, occurs at the level of the dimer, and results in a preferential incorporation of the functionally critical GluA2 subunit. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Plasma membrane (IBA). Reason: GluA2 is a multi-pass plasma membrane channel subunit acting at synaptic and extrasynaptic surface membrane; plasma membrane is the appropriate general location, with postsynaptic density membrane as the synaptic sub-location. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0005886 plasma membrane | IDA PMID:21846932 Mechanism of AMPA receptor activation by partial agonists: d... | ACCEPT | Summary: Plasma membrane (IDA). Reason: GluA2 is a multi-pass plasma membrane channel subunit acting at synaptic and extrasynaptic surface membrane; plasma membrane is the appropriate general location, with postsynaptic density membrane as the synaptic sub-location. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Plasma membrane (IEA). Reason: GluA2 is a multi-pass plasma membrane channel subunit acting at synaptic and extrasynaptic surface membrane; plasma membrane is the appropriate general location, with postsynaptic density membrane as the synaptic sub-location. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0005886 plasma membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Plasma membrane (ISO). Reason: GluA2 is a multi-pass plasma membrane channel subunit acting at synaptic and extrasynaptic surface membrane; plasma membrane is the appropriate general location, with postsynaptic density membrane as the synaptic sub-location. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0005886 plasma membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Plasma membrane (ISO). Reason: GluA2 is a multi-pass plasma membrane channel subunit acting at synaptic and extrasynaptic surface membrane; plasma membrane is the appropriate general location, with postsynaptic density membrane as the synaptic sub-location. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0005886 plasma membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Plasma membrane (ISS). Reason: GluA2 is a multi-pass plasma membrane channel subunit acting at synaptic and extrasynaptic surface membrane; plasma membrane is the appropriate general location, with postsynaptic density membrane as the synaptic sub-location. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0005886 plasma membrane | TAS Reactome:R-RNO-9022366 | ACCEPT | Summary: Plasma membrane (TAS). Reason: GluA2 is a multi-pass plasma membrane channel subunit acting at synaptic and extrasynaptic surface membrane; plasma membrane is the appropriate general location, with postsynaptic density membrane as the synaptic sub-location. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0006811 monoatomic ion transport | IEA GO_REF:0000002 | MODIFY | Summary: Monoatomic ion transport (IEA, InterPro). Reason: Correct but general; the channel mediates cation transmembrane flux. Refine to GO:0098655 monoatomic cation transmembrane transport, a descendant the gene carries. Proposed replacements: monoatomic cation transmembrane transport Supporting Evidence: file:rat/Gria2/Gria2-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:0007268 chemical synaptic transmission | IDA PMID:12554656 Regulated delivery of AMPA receptor subunits to the presynap... | MODIFY | Summary: Chemical synaptic transmission (IDA, presynaptic/growth cone AMPAR study). Reason: True but general; GluA2 receptors mediate glutamatergic transmission. Refine to GO:0035249 synaptic transmission, glutamatergic (is_a descendant, carried by IBA). 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:0007268 chemical synaptic transmission | ISO GO_REF:0000121 | MODIFY | Summary: Chemical synaptic transmission (ISO from mouse Gria2). Reason: Transfer is sound; refine to GO:0035249 synaptic transmission, glutamatergic (is_a descendant carried by IBA). Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95809 SUPPORTS TRANSFER Mouse Gria2 ortholog; only granularity 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:0008021 synaptic vesicle | ISO GO_REF:0000121 | MODIFY | Summary: Synaptic vesicle (ISO from mouse Gria2). Reason: GluA2 is an integral membrane protein, so its synaptic vesicle pool is in the vesicle membrane (copurification of GluR2 with small synaptic vesicles). Refine to GO:0030672 synaptic vesicle membrane (part_of descendant, carried by IDA). Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95809 SUPPORTS TRANSFER Mouse Gria2 ortholog; membrane sub-location refined. Proposed replacements: synaptic vesicle membrane Supporting Evidence: PMID:12554656 These data indicate that, at steady state, a major pool of AMPA receptor subunits reside in synaptic vesicle membranes and can be recruited to the presynaptic membrane as functional receptors in response to depolarization. |
| GO:0008092 cytoskeletal protein binding | IPI PMID:18297063 Inhibition of Arp2/3-mediated actin polymerization by PICK1 ... | MARK AS OVER ANNOTATED | Summary: Cytoskeletal protein binding (IPI with Arpc2), from the PICK1/Arp2/3 study. Reason: The paper shows PICK1 binds the Arp2/3 complex directly; GluR2 co-immunoprecipitates with Arp2/3 only as part of a PICK1-containing complex. There is no evidence that GluA2 itself binds Arp2/3 or actin. Supporting Evidence: PMID:18297063 co-immunoprecipitations from neuronal extract demonstrate an interaction between Arp2/3, PICK1 and GluR2 in native tissue (Fig. 1f) PMID:18297063 A pull-down assay using GST-PICK1 and purified Arp2/3 complex indicates that these proteins can interact directly (Fig. 1e) |
| GO:0008328 ionotropic glutamate receptor complex | TAS PMID:11836517 The structure and function of glutamate receptor ion channel... | MODIFY | Summary: Ionotropic glutamate receptor complex (TAS, review). Reason: Correct but general; refine to GO:0032281 AMPA glutamate receptor complex (is_a descendant, carried by IBA/IDA). Proposed replacements: AMPA glutamate receptor complex Supporting Evidence: PMID:11836517 Recent crystallographic analyses of the ligand-binding domains of these receptors have identified conformational changes associated with agonist binding PMID:30872532 the principal AMPAR complex at hippocampal synapses |
| 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 GluR2 detection in NAc neurons. Reason: GluA2 has a large extracellular domain and is detected on the cell surface by surface labelling; this is a valid but peripheral restatement of its plasma membrane location. 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 (IDA), surface biotinylation of GluR2 in hippocampal neurons subjected to OGD. Reason: Full text read: surface biotinylation shows GluR2 at the neuronal surface and its PICK1-dependent removal during oxygen/glucose deprivation. Surface location is real; plasma membrane is the more exact location, so this is kept as non-core. Supporting Evidence: PMID:19321442 We observed a time-dependent reduction in GluR2 surface expression by OGD |
| GO:0009986 cell surface | IDA PMID:24712995 BDNF contributes to both rapid and homeostatic alterations i... | KEEP AS NON CORE | Summary: Cell surface (IDA), BDNF regulation of surface GluA2 in NAc neurons. Reason: Surface GluA2 detected by immunocytochemistry and crosslinking; valid but peripheral to the plasma membrane location. 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:0010226 response to lithium ion | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Response to lithium ion (IEA). Reason: Based on changes in synaptic AMPA receptor subunit levels after chronic lithium; the cited abstract reports this for GluR1. An expression or trafficking change in response to a drug does not show that GluA2 carries out a response to lithium. 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 (IEP). Reason: Based on changes in synaptic AMPA receptor subunit levels after chronic lithium; the cited abstract reports this for GluR1. An expression or trafficking change in response to a drug does not show that GluA2 carries out a response to lithium. 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:0014069 postsynaptic density | IDA PMID:10701825 Differential synaptic localization of the glutamate transpor... | MODIFY | Summary: Postsynaptic density (IDA). Reason: GluA2 is an integral membrane protein at the PSD; the more exact location is GO:0098839 postsynaptic density membrane (part_of descendant), which the gene carries by IBA and IDA. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. |
| GO:0014069 postsynaptic density | IDA PMID:28057533 Presynaptic PICK1 facilitates trafficking of AMPA-receptors ... | MODIFY | Summary: Postsynaptic density (IDA). Reason: GluA2 is an integral membrane protein at the PSD; the more exact location is GO:0098839 postsynaptic density membrane (part_of descendant), which the gene carries by IBA and IDA. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. |
| GO:0014069 postsynaptic density | IDA PMID:32948689 GRIP1 regulates synaptic plasticity and learning and memory. | MODIFY | Summary: Postsynaptic density (IDA). Reason: GluA2 is an integral membrane protein at the PSD; the more exact location is GO:0098839 postsynaptic density membrane (part_of descendant), which the gene carries by IBA and IDA. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0014069 postsynaptic density | ISO GO_REF:0000121 | MODIFY | Summary: Postsynaptic density (ISO from mouse Gria2). Reason: Transfer is sound; refine to the membrane sub-location GO:0098839 postsynaptic density membrane. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95809 SUPPORTS TRANSFER Mouse Gria2 ortholog; membrane sub-location refined. Proposed replacements: postsynaptic density membrane Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. |
| 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 (is_a descendant). Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: file:rat/Gria2/Gria2-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:0015277 kainate selective glutamate receptor activity | IDA PMID:21846932 Mechanism of AMPA receptor activation by partial agonists: d... | MODIFY | Summary: Kainate selective glutamate receptor activity (IDA), from disulfide-trapping of GluA2 ligand-binding domain with partial agonists. Reason: Full text read. The study uses kainate as a weak partial agonist of the AMPA receptor GluA2, not as evidence of a kainate-selective receptor; GO:0015277 describes kainate-type receptors (GluK1-5). The correct activity is GO:0004971 AMPA glutamate receptor activity. Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:21846932 the weak partial agonist kainate presents a structural impediment to lobe closure PMID:21846932 The ligand-binding domain of AMPA receptors is a bilobed structure, and the closure of the lobes is associated with channel activation. file:rat/Gria2/Gria2-uniprot.txt This receptor binds AMPA (quisqualate) > L-glutamate > kainate |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Membrane (IEA, InterPro). Reason: Correct but general; GluA2 is a plasma membrane channel. Refine to GO:0005886 plasma membrane. Proposed replacements: plasma membrane Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. |
| GO:0016020 membrane | ISO GO_REF:0000121 | MODIFY | Summary: Membrane (ISO from mouse Gria2). Reason: Correct but general; refine to GO:0005886 plasma membrane. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95809 SUPPORTS TRANSFER Mouse Gria2 ortholog; location refined. Proposed replacements: plasma membrane Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. |
| GO:0019722 calcium-mediated signaling | IEA GO_REF:0000108 | REMOVE | Summary: Calcium-mediated signaling (IEA, inferred from glutamate-gated calcium channel activity). Reason: Inherited from GO:0022849, which rests on unedited or mutant GluA2 constructs. Native GluA2 is Q/R-edited and makes AMPA receptors Ca2+-impermeable; GluA2 is the subunit that prevents AMPAR-mediated Ca2+ entry, so a Ca2+-signalling role is the opposite of its physiological contribution. Supporting Evidence: file:rat/Gria2/Gria2-uniprot.txt Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent cations. |
| GO:0019865 immunoglobulin binding | IPI PMID:26595655 Synaptic adhesion molecule IgSF11 regulates synaptic transmi... | MODIFY | Summary: Immunoglobulin binding (IPI with IgSF11). Reason: Full text read. The partner IgSF11 is an immunoglobulin-superfamily synaptic adhesion molecule, not an immunoglobulin; GO:0019865 is defined by binding an immunoglobulin complex. The co-immunoprecipitation of IgSF11 with GluA1/GluA2 in rat brain supports 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 (Fig. 2a). |
| GO:0019865 immunoglobulin binding | IPI PMID:26595655 Synaptic adhesion molecule IgSF11 regulates synaptic transmi... | MODIFY | Summary: Immunoglobulin binding (IPI with IgSF11). Reason: Full text read. The partner IgSF11 is an immunoglobulin-superfamily synaptic adhesion molecule, not an immunoglobulin; GO:0019865 is defined by binding an immunoglobulin complex. The co-immunoprecipitation of IgSF11 with GluA1/GluA2 in rat brain supports 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 (Fig. 2a). |
| 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 GSK3B), from the GSK3beta LTP/LTD study. Reason: The cached abstract does not mention GluA2 and the full text is not available, so the interaction with GSK3B cannot be checked here. It is not independently established for this gene. |
| 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), from developmental expression of AMPAR and PDZ proteins in neocortex. Reason: Expression timing during cortical development is not evidence that GluA2 carries out cortex development. 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:0022849 glutamate-gated calcium ion channel activity | IDA PMID:11773314 Voltage and concentration dependence of Ca(2+) permeability ... | MARK AS OVER ANNOTATED | Summary: Glutamate-gated calcium ion channel activity (IDA). Reason: Ca2+ permeation in the cited study was measured on GluA1(Q) and on unedited GluR-B(Q) or mutant GluR-B(N) constructs. Native GluA2 is almost completely Q/R-edited, and edited GluA2 makes AMPA receptors Ca2+-impermeable; Ca2+-permeable AMPARs are defined by lacking GluA2. The claim overstates the physiological property of the gene product. Supporting Evidence: PMID:11773314 recombinant NMDAR NR1-NR2A, AMPAR GluR-A(Q) and KAR GluR-6(Q) channels PMID:11773314 than that in unedited GluR-B(Q) channels file:rat/Gria2/Gria2-uniprot.txt Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent cations. |
| GO:0022849 glutamate-gated calcium ion channel activity | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Glutamate-gated calcium ion channel activity (IEA). Reason: Ca2+ permeation in the cited study was measured on GluA1(Q) and on unedited GluR-B(Q) or mutant GluR-B(N) constructs. Native GluA2 is almost completely Q/R-edited, and edited GluA2 makes AMPA receptors Ca2+-impermeable; Ca2+-permeable AMPARs are defined by lacking GluA2. The claim overstates the physiological property of the gene product. Supporting Evidence: file:rat/Gria2/Gria2-uniprot.txt Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent cations. |
| GO:0030165 PDZ domain binding | IDA PMID:10558890 rDLG6: a novel homolog of Drosophila DLG expressed in rat br... | ACCEPT | Summary: PDZ domain binding. The GluA2 C-terminal -SVKI motif binds class II PDZ domains of GRIP1/ABP/GRIP2, PICK1 and MAGUKs. Reason: Core trafficking function: the C-terminal PDZ ligand of GluA2 binds PDZ domains of GRIP1/2 (ABP) and PICK1, which anchor, cluster and recycle AMPA receptors; binding is regulated by Ser880 and Tyr876 phosphorylation. Supporting Evidence: PMID:10558890 GST pull-down assays showed that the PDZ domain of rDLG6 protein binds to the C-terminus of the AMPA (alpha-Amino-3-hydroxy-5-Methyl-isoxazole-4-Propionic Acid) receptor GluR2 subunit. |
| GO:0030165 PDZ domain binding | IPI PMID:10027300 Clustering of AMPA receptors by the synaptic PDZ domain-cont... | ACCEPT | Summary: PDZ domain binding. The GluA2 C-terminal -SVKI motif binds class II PDZ domains of GRIP1/ABP/GRIP2, PICK1 and MAGUKs. Reason: Core trafficking function: the C-terminal PDZ ligand of GluA2 binds PDZ domains of GRIP1/2 (ABP) and PICK1, which anchor, cluster and recycle AMPA receptors; binding is regulated by Ser880 and Tyr876 phosphorylation. Supporting Evidence: PMID:10027300 Here, we show that PICK1 (protein interacting with C kinase), a PDZ domain-containing protein, interacts with the C termini of alpha-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA) receptors in vitro and in vivo. |
| GO:0030165 PDZ domain binding | IPI PMID:9697854 NSF binding to GluR2 regulates synaptic transmission. | ACCEPT | Summary: PDZ domain binding. The GluA2 C-terminal -SVKI motif binds class II PDZ domains of GRIP1/ABP/GRIP2, PICK1 and MAGUKs. Reason: Core trafficking function: the C-terminal PDZ ligand of GluA2 binds PDZ domains of GRIP1/2 (ABP) and PICK1, which anchor, cluster and recycle AMPA receptors; binding is regulated by Ser880 and Tyr876 phosphorylation. Supporting Evidence: PMID:9069286 Here we identify a synaptic PDZ domain-containing protein GRIP (glutamate receptor interacting protein) that specifically interacts with the C termini of AMPA receptors. PMID:9768844 ABP binds to the GluR2/3 C-terminal VKI-COOH motif via class II hydrophobic PDZ interactions |
| GO:0030424 axon | IDA PMID:16157387 Generation of lentiviral transgenic rats expressing glutamat... | KEEP AS NON CORE | Summary: Axon (IDA), GRIP1 transgenic rat study. Reason: GluA2 is mainly somatodendritic, but axonal pools exist (growth cones, presynaptic terminals). Peripheral location. Supporting Evidence: PMID:12554656 We demonstrate that the AMPA receptor subunits GluR1 and GluR2 are expressed and organized in functional receptors in axonal growth cones of hippocampal neurons. |
| GO:0030425 dendrite | IDA PMID:10701825 Differential synaptic localization of the glutamate transpor... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0030425 dendrite | IDA PMID:12629171 Interaction between liprin-alpha and GIT1 is required for AM... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:12629171 Expression of dominant-negative constructs interfering with the GIT1-liprin-alpha interaction leads to a selective and marked reduction in the dendritic and surface clustering of AMPA receptors in cultured neurons. |
| GO:0030425 dendrite | IDA PMID:15844209 Ionotropic glutamate receptors are expressed in GABAergic te... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:15844209 28% are immunopositive using an antibody for the GluR2/4 subunits of the AMPA receptor |
| GO:0030425 dendrite | IDA PMID:15965473 GRIP1 controls dendrite morphogenesis by regulating EphB rec... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:15965473 caused a loss of dendrites, associated with mislocalization of the GRIP-interacting proteins GIuR2 (AMPA receptor subunit) |
| GO:0030425 dendrite | IDA PMID:20032460 Inhibition of calcineurin-mediated endocytosis and alpha-ami... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:20032460 we found that ADDLs interact preferentially with GluR2-containing complexes. |
| GO:0030425 dendrite | IDA PMID:21807099 mGluR and NMDAR activation internalize distinct populations ... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:21807099 we immunolabeled surface GluA2s and the presynaptic marker synapsin in control and agonist treated neurons. |
| GO:0030425 dendrite | IDA PMID:21847098 PIKE-mediated PI3-kinase activity is required for AMPA recep... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:21847098 PIKE-L directly interacts with both GluA2 and GRIP1 and forms a tertiary complex upon glycine-induced NMDA receptor activation. |
| GO:0030425 dendrite | IDA PMID:26109571 Activity-dependent synaptic GRIP1 accumulation drives synapt... | KEEP AS NON CORE | Summary: Dendrite (IDA), immunolocalization in cultured or in situ neurons. Reason: GluA2 is distributed through dendritic shafts and spines, including intracellular pools; dendrite is as precise as these assays allow. The functional site is the postsynaptic density membrane of spines, so this is non-core. Supporting Evidence: PMID:26109571 scaling up requires the interaction between GRIP1 and GluA2. |
| GO:0030425 dendrite | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Dendrite (ISO from mouse Gria2). Reason: Consistent with the rat IDA rows; somatodendritic localization is well established. Non-core. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0030426 growth cone | IDA PMID:12554656 Regulated delivery of AMPA receptor subunits to the presynap... | KEEP AS NON CORE | Summary: Growth cone (IDA). Reason: Functional AMPA receptors containing GluR2 are present in axonal growth cones of developing hippocampal neurons; developmental, non-core location. Supporting Evidence: PMID:12554656 We demonstrate that the AMPA receptor subunits GluR1 and GluR2 are expressed and organized in functional receptors in axonal growth cones of hippocampal neurons. |
| GO:0030672 synaptic vesicle membrane | IDA PMID:12554656 Regulated delivery of AMPA receptor subunits to the presynap... | KEEP AS NON CORE | Summary: Synaptic vesicle membrane (IDA). Reason: GluR2 copurifies with small synaptic vesicles and is recruited to the presynaptic membrane on depolarization; a presynaptic pool, non-core. Supporting Evidence: PMID:12554656 These data indicate that, at steady state, a major pool of AMPA receptor subunits reside in synaptic vesicle membranes and can be recruited to the presynaptic membrane as functional receptors in response to depolarization. |
| GO:0030672 synaptic vesicle membrane | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Synaptic vesicle membrane (ISO from mouse Gria2). Reason: Consistent with rat IDA evidence for a vesicular presynaptic pool; non-core. Supporting Evidence: PMID:12554656 These data indicate that, at steady state, a major pool of AMPA receptor subunits reside in synaptic vesicle membranes and can be recruited to the presynaptic membrane as functional receptors in response to depolarization. PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. |
| GO:0031623 receptor internalization | IDA PMID:10856222 Disruption of AMPA receptor GluR2 clusters following long-te... | KEEP AS NON CORE | Summary: Receptor internalization (IDA). Reason: GluA2 undergoes constitutive and regulated endocytosis, and its own cytoplasmic tail contributes to it by binding AP-2 and by phosphorylation-controlled release from GRIP; the endocytosis of GluA2-containing receptors expresses LTD. A real process role, but a trafficking step of the receptor rather than its channel function, so non-core. Supporting Evidence: PMID:10856222 Moreover, GluR2 protein released from GRIP is shown to be internalized. PMID:17289840 an atypical basic motif within the cytoplasmic tails of AMPA-type glutamate receptors directly associates with mu2-adaptin |
| GO:0031623 receptor internalization | IDA PMID:11100149 Distinct molecular mechanisms and divergent endocytotic path... | KEEP AS NON CORE | Summary: Receptor internalization (IDA). Reason: GluA2 undergoes constitutive and regulated endocytosis, and its own cytoplasmic tail contributes to it by binding AP-2 and by phosphorylation-controlled release from GRIP; the endocytosis of GluA2-containing receptors expresses LTD. A real process role, but a trafficking step of the receptor rather than its channel function, so non-core. Supporting Evidence: PMID:11100149 sequence determinants within the cytoplasmic tails of GluR1 and GluR2 subunits PMID:17289840 an atypical basic motif within the cytoplasmic tails of AMPA-type glutamate receptors directly associates with mu2-adaptin |
| GO:0032279 asymmetric synapse | IDA PMID:10701825 Differential synaptic localization of the glutamate transpor... | KEEP AS NON CORE | Summary: Asymmetric synapse (IDA, immunogold EM). Reason: GluA2 is concentrated at asymmetric (excitatory) synapses; valid, with glutamatergic synapse as the main synaptic term. Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. |
| GO:0032279 asymmetric synapse | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | KEEP AS NON CORE | Summary: Asymmetric synapse (IDA, immunogold EM). Reason: GluA2 is concentrated at asymmetric (excitatory) synapses; valid, with glutamatergic synapse as the main synaptic term. Supporting Evidence: PMID:12077196 AMPAR immunoreactivity was also detectable at most synapses; its distribution was independent of that of alpha7nAChR. |
| GO:0032281 AMPA glutamate receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: AMPA glutamate receptor complex (IBA). Reason: GluA2 is a core subunit of homo- and heteromeric AMPA receptor complexes together with TARP and cornichon auxiliary subunits. Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. |
| GO:0032281 AMPA glutamate receptor complex | IDA PMID:19265014 Functional proteomics identify cornichon proteins as auxilia... | ACCEPT | Summary: AMPA glutamate receptor complex (IDA). Reason: GluA2 is a core subunit of homo- and heteromeric AMPA receptor complexes together with TARP and cornichon auxiliary subunits. 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 | IDA PMID:19946266 X-ray structure, symmetry and mechanism of an AMPA-subtype g... | ACCEPT | Summary: AMPA glutamate receptor complex (IDA). Reason: GluA2 is a core subunit of homo- and heteromeric AMPA receptor complexes together with TARP and cornichon auxiliary subunits. Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. |
| GO:0032281 AMPA glutamate receptor complex | IEA GO_REF:0000117 | ACCEPT | Summary: AMPA glutamate receptor complex (IEA). Reason: GluA2 is a core subunit of homo- and heteromeric AMPA receptor complexes together with TARP and cornichon auxiliary subunits. Supporting Evidence: file:rat/Gria2/Gria2-uniprot.txt Homotetramer or heterotetramer of pore-forming glutamate receptor subunits |
| 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 (IPI). Reason: GluA2 is a core subunit of homo- and heteromeric AMPA receptor complexes together with TARP and cornichon auxiliary subunits. Supporting Evidence: PMID:30872532 the principal AMPAR complex at hippocampal synapses |
| GO:0032281 AMPA glutamate receptor complex | ISO GO_REF:0000121 | ACCEPT | Summary: AMPA glutamate receptor complex (ISO). Reason: GluA2 is a core subunit of homo- and heteromeric AMPA receptor complexes together with TARP and cornichon auxiliary subunits. Supporting Evidence: PMID:30872532 the principal AMPAR complex at hippocampal synapses |
| GO:0032590 dendrite membrane | IDA PMID:11931740 Interaction between GRIP and liprin-alpha/SYD2 is required f... | KEEP AS NON CORE | Summary: Dendrite membrane (IDA). Reason: Surface GluA2 in dendrites, consistent with interference studies of GRIP-liprin targeting. Valid peripheral location. Supporting Evidence: PMID:11931740 Dominant-negative constructs that interfere with the GRIP-liprin interaction disrupt the surface expression and dendritic clustering of AMPA receptors in cultured neurons. |
| GO:0032839 dendrite cytoplasm | IDA PMID:17207780 Distribution of NMDA and AMPA receptor subunits at thalamo-a... | KEEP AS NON CORE | Summary: Dendrite cytoplasm (IDA), immunogold EM of thalamo-amygdaloid spines. Reason: Reflects intracellular (vesicular/endosomal) pools of GluA2 in spines; GluA2 is a membrane protein, so this denotes internal membranes in the dendritic cytoplasm. Non-core. Supporting Evidence: PMID:17207780 Analyses revealed that the cytoplasmic pool of GluR2 receptors was twice as large compared to the GluR3, NR1, and NR2B subunits. |
| GO:0032991 protein-containing complex | IDA PMID:17329210 LTP inhibits LTD in the hippocampus via regulation of GSK3be... | TOO GENERAL | Summary: Protein-containing complex. Reason: True but uninformative: GluA2 is part of the AMPA glutamate receptor complex (GO:0032281, accepted in this review), which entails this term. The cited complexes (with PICK1 or GSK3B) are trafficking/signalling assemblies. Supporting Evidence: PMID:30872532 the principal AMPAR complex at hippocampal synapses |
| GO:0032991 protein-containing complex | IPI PMID:10027300 Clustering of AMPA receptors by the synaptic PDZ domain-cont... | TOO GENERAL | Summary: Protein-containing complex. Reason: True but uninformative: GluA2 is part of the AMPA glutamate receptor complex (GO:0032281, accepted in this review), which entails this term. The cited complexes (with PICK1 or GSK3B) are trafficking/signalling assemblies. Supporting Evidence: PMID:10027300 Here, we show that PICK1 (protein interacting with C kinase), a PDZ domain-containing protein, interacts with the C termini of alpha-amino-3-hydroxy-5-methyl-isoxazole-4-propionic acid (AMPA) receptors in vitro and in vivo. |
| GO:0034220 monoatomic ion transmembrane transport | IEA GO_REF:0000120 | MODIFY | Summary: Monoatomic ion transmembrane transport (IEA). Reason: Correct but general; refine to GO:0098655 monoatomic cation transmembrane transport (descendant). Proposed replacements: monoatomic cation transmembrane transport Supporting Evidence: file:rat/Gria2/Gria2-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:0035235 ionotropic glutamate receptor signaling pathway | ISO GO_REF:0000121 | ACCEPT | Summary: Ionotropic glutamate receptor signaling pathway (ISO). Reason: GluA2-containing AMPA receptors transduce glutamate binding into cation influx and depolarization; this pathway term fits the receptor. Supporting Evidence: file:rat/Gria2/Gria2-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:30872532 Within the receptor, the core subunits arrange to give the GluA2 subunit dominant control of gating. |
| GO:0035235 ionotropic glutamate receptor signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: Ionotropic glutamate receptor signaling pathway (ISS). Reason: GluA2-containing AMPA receptors transduce glutamate binding into cation influx and depolarization; this pathway term fits the receptor. Supporting Evidence: file:rat/Gria2/Gria2-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:30872532 Within the receptor, the core subunits arrange to give the GluA2 subunit dominant control of gating. |
| 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). Reason: GluA2-containing AMPA receptors transduce glutamate binding into cation influx and depolarization; this pathway term fits the receptor. Supporting Evidence: file:rat/Gria2/Gria2-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:30872532 Within the receptor, the core subunits arrange to give the GluA2 subunit dominant control of gating. |
| GO:0035249 synaptic transmission, glutamatergic | IBA GO_REF:0000033 | ACCEPT | Summary: Synaptic transmission, glutamatergic (IBA). Reason: Core process: AMPA receptors containing GluA2 mediate most fast excitatory glutamatergic transmission; interfering with GluA2 trafficking alters AMPAR-mediated EPSCs. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:9697854 Loading of decapeptides corresponding to the NSF-binding domain of GluR2 into rat hippocampal CA1 pyramidal neurons results in a marked, progressive decrement of AMPA receptor-mediated synaptic transmission. |
| 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 GluA1), NTD structural study. Reason: GluA2 binds GluA1 through its NTD and LBD to form heteromeric AMPA receptors; this is assembly of the receptor complex, kept as non-core. Supporting Evidence: PMID:21639859 Comparative analyses of the structure of GluA1-ATD and other subunits sheds light on our understanding of how ATD drives subfamily-specific assembly of AMPARs. PMID:19461580 Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers |
| GO:0035255 ionotropic glutamate receptor binding | IPI PMID:10414981 Association of AMPA receptors with a subset of glutamate rec... | KEEP AS NON CORE | Summary: Ionotropic glutamate receptor binding (IPI with GluN1 or GluA1). Reason: GluA2 assembles with other ionotropic glutamate receptor subunits (GluA1) and co-purifies in synaptic complexes. Non-core assembly interaction. Supporting Evidence: PMID:10414981 A majority of detergent-extractable GluR2/3 was complexed with GRIP in the brain. PMID:19461580 Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers |
| GO:0035255 ionotropic glutamate receptor binding | IPI PMID:10414981 Association of AMPA receptors with a subset of glutamate rec... | KEEP AS NON CORE | Summary: Ionotropic glutamate receptor binding (IPI with GluN1 or GluA1). Reason: GluA2 assembles with other ionotropic glutamate receptor subunits (GluA1) and co-purifies in synaptic complexes. Non-core assembly interaction. Supporting Evidence: PMID:10414981 A majority of detergent-extractable GluR2/3 was complexed with GRIP in the brain. PMID:19461580 Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers |
| GO:0036477 somatodendritic compartment | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Somatodendritic compartment (ISO). Reason: GluA2 shows somatodendritic localization in neurons; valid peripheral location. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0038023 signaling receptor activity | IDA PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | MODIFY | Summary: Signaling receptor activity (IDA). Reason: Correct but general; refine to GO:0004971 AMPA glutamate receptor activity (is_a descendant the gene carries). Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0038023 signaling receptor activity | IEA GO_REF:0000002 | MODIFY | Summary: Signaling receptor activity (IEA). Reason: Correct but general; refine to GO:0004971 AMPA glutamate receptor activity (is_a descendant the gene carries). Proposed replacements: AMPA glutamate receptor activity Supporting Evidence: file:rat/Gria2/Gria2-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:0042734 presynaptic membrane | IDA PMID:12554656 Regulated delivery of AMPA receptor subunits to the presynap... | KEEP AS NON CORE | Summary: Presynaptic membrane (IDA). Reason: Presynaptic AMPA receptors containing GluA2 occur at some terminals (corticostriatal, Schaffer collateral, hippocampal growth cones/terminals); real but secondary to the postsynaptic role. Supporting Evidence: PMID:12554656 These data indicate that, at steady state, a major pool of AMPA receptor subunits reside in synaptic vesicle membranes and can be recruited to the presynaptic membrane as functional receptors in response to depolarization. |
| GO:0042734 presynaptic membrane | IDA PMID:15610164 Presynaptic localization of an AMPA-type glutamate receptor ... | KEEP AS NON CORE | Summary: Presynaptic membrane (IDA). Reason: Presynaptic AMPA receptors containing GluA2 occur at some terminals (corticostriatal, Schaffer collateral, hippocampal growth cones/terminals); real but secondary to the postsynaptic role. 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:0042734 presynaptic membrane | IDA PMID:16903873 Ultrastructural localisation and differential agonist-induce... | KEEP AS NON CORE | Summary: Presynaptic membrane (IDA). Reason: Presynaptic AMPA receptors containing GluA2 occur at some terminals (corticostriatal, Schaffer collateral, hippocampal growth cones/terminals); real but secondary to the postsynaptic role. 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 (IEP). Reason: The location is supported by the same synaptosome fractionation and by other immunogold studies, so the row is kept like the other presynaptic membrane rows. An expression-pattern code cannot by itself establish a location, so the evidence code is flagged upstream. 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: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:0042802 identical protein binding | IPI PMID:19461580 Crystal structure and association behaviour of the GluR2 ami... | KEEP AS NON CORE | Summary: Identical protein binding (IPI, GluA2-GluA2). Reason: GluA2 forms homodimers through its ATD and LBD and assembles into homotetramers; this self-association underlies receptor assembly and is kept as non-core. 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:19617541 Energetics of glutamate receptor ligand binding domain dimer... | KEEP AS NON CORE | Summary: Identical protein binding (IPI, GluA2-GluA2). Reason: GluA2 forms homodimers through its ATD and LBD and assembles into homotetramers; this self-association underlies receptor assembly and is kept as non-core. The cited study is mainly on kainate (GluK2) and delta2 LBD dimers; abstract-only, so its GluA2 content cannot be checked, but the claim is independently established. 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 (IPI, GluA2-GluA2). Reason: GluA2 forms homodimers through its ATD and LBD and assembles into homotetramers; this self-association underlies receptor assembly and is kept as non-core. Supporting Evidence: PMID:21317873 Heteromerization is dominant, occurs at the level of the dimer, and results in a preferential incorporation of the functionally critical GluA2 subunit. |
| GO:0042802 identical protein binding | IPI PMID:24673938 L-Asp is a useful tool in the purification of the ionotropic... | KEEP AS NON CORE | Summary: Identical protein binding (IPI, GluA2-GluA2). Reason: GluA2 forms homodimers through its ATD and LBD and assembles into homotetramers; this self-association underlies receptor assembly and is kept as non-core. Supporting Evidence: PMID:24673938 Surprisingly, with 7.5 mM L-Asp, the GluA2 LBD crystallized as a mixed dimer |
| GO:0042802 identical protein binding | IPI PMID:31925409 Cryo-EM structures of the ionotropic glutamate receptor GluD... | KEEP AS NON CORE | Summary: Identical protein binding (IPI, GluA2-GluA2). Reason: GluA2 forms homodimers through its ATD and LBD and assembles into homotetramers; this self-association underlies receptor assembly and is kept as non-core. Full text read: PMID:31925409 is a cryo-EM study of GluD1 and does not mention GluA2; the row appears to belong to rat Grid1. The claim itself is supported by other studies. Supporting Evidence: PMID:19461580 Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers |
| GO:0043005 neuron projection | ISO GO_REF:0000121 | MODIFY | Summary: Neuron projection (ISO). Reason: Correct but general; GluA2 is somatodendritic and acts in dendrites/spines. Refine to GO:0030425 dendrite (is_a descendant carried by IDA). Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95809 SUPPORTS TRANSFER Mouse Gria2 ortholog; location refined. Proposed replacements: dendrite Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043025 neuronal cell body | IDA PMID:10414981 Association of AMPA receptors with a subset of glutamate rec... | KEEP AS NON CORE | Summary: Neuronal cell body (IDA). Reason: GluA2 is present in somata (biosynthetic and trafficking pools); valid but not the site of synaptic function. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043025 neuronal cell body | IDA PMID:10701825 Differential synaptic localization of the glutamate transpor... | KEEP AS NON CORE | Summary: Neuronal cell body (IDA). Reason: GluA2 is present in somata (biosynthetic and trafficking pools); valid but not the site of synaptic function. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043025 neuronal cell body | IDA PMID:11100149 Distinct molecular mechanisms and divergent endocytotic path... | KEEP AS NON CORE | Summary: Neuronal cell body (IDA). Reason: GluA2 is present in somata (biosynthetic and trafficking pools); valid but not the site of synaptic function. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043025 neuronal cell body | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | KEEP AS NON CORE | Summary: Neuronal cell body (IDA). Reason: GluA2 is present in somata (biosynthetic and trafficking pools); valid but not the site of synaptic function. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043025 neuronal cell body | IDA PMID:15844209 Ionotropic glutamate receptors are expressed in GABAergic te... | KEEP AS NON CORE | Summary: Neuronal cell body (IDA). Reason: GluA2 is present in somata (biosynthetic and trafficking pools); valid but not the site of synaptic function. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043025 neuronal cell body | IDA PMID:16157387 Generation of lentiviral transgenic rats expressing glutamat... | KEEP AS NON CORE | Summary: Neuronal cell body (IDA). Reason: GluA2 is present in somata (biosynthetic and trafficking pools); valid but not the site of synaptic function. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| 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 (IDA). Reason: GluA2 is present in somata (biosynthetic and trafficking pools); valid but not the site of synaptic function. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043025 neuronal cell body | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Neuronal cell body (IEA). Reason: Consistent with IDA rows; non-core. Supporting Evidence: PMID:10701825 Both GluR2 and EAAC1 are present in the dendritic membranes and cytoplasm |
| GO:0043195 terminal bouton | IDA PMID:15844209 Ionotropic glutamate receptors are expressed in GABAergic te... | KEEP AS NON CORE | Summary: Terminal bouton (IDA), GluR2/4 immunoreactivity in GABAergic terminals of dorsal horn. Reason: Presynaptic AMPARs in specific terminals; peripheral location. Supporting Evidence: PMID:15844209 28% are immunopositive using an antibody for the GluR2/4 subunits of the AMPA receptor |
| GO:0043197 dendritic spine | IBA GO_REF:0000033 | ACCEPT | Summary: Dendritic spine (IBA). Reason: Most excitatory synapses on principal neurons are on spines, where GluA2-containing AMPARs are anchored at the PSD membrane; GluA2 is detected in the large majority of spines. Supporting Evidence: PMID:17207780 A high percentage of thalamo-amygdaloid spines was immunoreactive for GluR2 (80%) |
| GO:0043197 dendritic spine | IDA PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | ACCEPT | Summary: Dendritic spine (IDA). Reason: Most excitatory synapses on principal neurons are on spines, where GluA2-containing AMPARs are anchored at the PSD membrane; GluA2 is detected in the large majority of spines. Supporting Evidence: PMID:17207780 A high percentage of thalamo-amygdaloid spines was immunoreactive for GluR2 (80%) |
| GO:0043197 dendritic spine | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | ACCEPT | Summary: Dendritic spine (IDA). Reason: Most excitatory synapses on principal neurons are on spines, where GluA2-containing AMPARs are anchored at the PSD membrane; GluA2 is detected in the large majority of spines. Supporting Evidence: PMID:12077196 AMPAR immunoreactivity was also detectable at most synapses; its distribution was independent of that of alpha7nAChR. |
| GO:0043197 dendritic spine | IDA PMID:16157387 Generation of lentiviral transgenic rats expressing glutamat... | ACCEPT | Summary: Dendritic spine (IDA). Reason: Most excitatory synapses on principal neurons are on spines, where GluA2-containing AMPARs are anchored at the PSD membrane; GluA2 is detected in the large majority of spines. Supporting Evidence: PMID:17207780 A high percentage of thalamo-amygdaloid spines was immunoreactive for GluR2 (80%) |
| GO:0043197 dendritic spine | IDA PMID:17207780 Distribution of NMDA and AMPA receptor subunits at thalamo-a... | ACCEPT | Summary: Dendritic spine (IDA). Reason: Most excitatory synapses on principal neurons are on spines, where GluA2-containing AMPARs are anchored at the PSD membrane; GluA2 is detected in the large majority of spines. Supporting Evidence: PMID:17207780 A high percentage of thalamo-amygdaloid spines was immunoreactive for GluR2 (80%) |
| GO:0043197 dendritic spine | IEA GO_REF:0000117 | ACCEPT | Summary: Dendritic spine (IEA). Reason: Most excitatory synapses on principal neurons are on spines, where GluA2-containing AMPARs are anchored at the PSD membrane; GluA2 is detected in the large majority of spines. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. |
| GO:0043198 dendritic shaft | IDA PMID:10414981 Association of AMPA receptors with a subset of glutamate rec... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IDA PMID:11007883 Phosphorylation of the AMPA receptor subunit GluR2 different... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IDA PMID:11100149 Distinct molecular mechanisms and divergent endocytotic path... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IDA PMID:11978826 Differential palmitoylation directs the AMPA receptor-bindin... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IDA PMID:12077196 Alpha7 nicotinic acetylcholine receptors occur at postsynapt... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IDA PMID:16157387 Generation of lentiviral transgenic rats expressing glutamat... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IDA PMID:19160501 Serine phosphorylation of ephrinB2 regulates trafficking of ... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IDA PMID:9697855 The AMPA receptor GluR2 C terminus can mediate a reversible,... | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043198 dendritic shaft | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Dendritic shaft (IDA/IEA). Reason: GluA2 is found in dendritic shafts (shaft synapses of interneurons, trafficking pools, phospho-S880 GluA2 with PICK1); valid but peripheral. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0043204 perikaryon | IDA PMID:15844209 Ionotropic glutamate receptors are expressed in GABAergic te... | KEEP AS NON CORE | Summary: Perikaryon (IDA). Reason: Somatic pool of GluA2; non-core. Supporting Evidence: PMID:15844209 28% are immunopositive using an antibody for the GluR2/4 subunits of the AMPA receptor |
| GO:0044326 dendritic spine neck | IDA PMID:11007883 Phosphorylation of the AMPA receptor subunit GluR2 different... | KEEP AS NON CORE | Summary: Dendritic spine neck (IDA). Reason: Sub-spine location of GluA2 pools; non-core. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0044327 dendritic spine head | IDA PMID:11007883 Phosphorylation of the AMPA receptor subunit GluR2 different... | KEEP AS NON CORE | Summary: Dendritic spine head (IDA). Reason: GluA2 is in spine heads where the PSD lies; dendritic spine and PSD membrane capture the functional site. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:0044327 dendritic spine head | IDA PMID:11978826 Differential palmitoylation directs the AMPA receptor-bindin... | KEEP AS NON CORE | Summary: Dendritic spine head (IDA). Reason: GluA2 is in spine heads where the PSD lies; dendritic spine and PSD membrane capture the functional site. Supporting Evidence: PMID:11978826 pABP-L is membrane targeted and associates with surface-localized GluR2 receptors at the plasma membrane in spines. |
| GO:0044877 protein-containing complex binding | IPI PMID:21847098 PIKE-mediated PI3-kinase activity is required for AMPA recep... | KEEP AS NON CORE | Summary: Protein-containing complex binding (IPI with GRIP1 and PIKE). Reason: GluA2 joins a GRIP1-PIKE-L complex after glycine-induced NMDAR activation; peripheral regulatory interaction. Supporting Evidence: PMID:21847098 PIKE-L directly interacts with both GluA2 and GRIP1 and forms a tertiary complex upon glycine-induced NMDA receptor activation. |
| GO:0045184 establishment of protein localization | IMP PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | MARK AS OVER ANNOTATED | Summary: Establishment of protein localization (IMP). Reason: GluA2 C-tail interactions determine where GluA2-containing receptors go; the receptor is the cargo whose localization is established, while NSF and PDZ proteins move and anchor it. Supporting Evidence: PMID:11348590 GluR2/GluR3 receptors replace existing synaptic receptors continuously; this occurs only at synapses that already have AMPA-Rs and requires interactions by GluR2 with NSF and group II PDZ domain proteins. |
| GO:0045202 synapse | IDA PMID:10027300 Clustering of AMPA receptors by the synaptic PDZ domain-cont... | MODIFY | Summary: Synapse (IDA). Reason: Correct but general; refine to GO:0098978 glutamatergic synapse (is_a descendant carried by IDA/ISO). Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:10027300 In neurons, PICK1 specifically colocalizes with AMPA receptors at excitatory synapses. |
| GO:0045202 synapse | ISO GO_REF:0000121 | MODIFY | Summary: Synapse (ISO). Reason: Correct but general; refine to GO:0098978 glutamatergic synapse. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:95809 SUPPORTS TRANSFER Mouse Gria2 ortholog; location refined. Proposed replacements: glutamatergic synapse Supporting Evidence: PMID:10027300 In neurons, PICK1 specifically colocalizes with AMPA receptors at excitatory synapses. |
| GO:0045211 postsynaptic membrane | IDA PMID:16903873 Ultrastructural localisation and differential agonist-induce... | ACCEPT | Summary: Postsynaptic membrane (IDA). Reason: GluA2-containing AMPARs act in the postsynaptic membrane of excitatory synapses (synaptic and perisynaptic). 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:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0045211 postsynaptic membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Postsynaptic membrane (IEA). Reason: GluA2-containing AMPARs act in the postsynaptic membrane of excitatory synapses (synaptic and perisynaptic). 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:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0045211 postsynaptic membrane | IEP PMID:16903873 Ultrastructural localisation and differential agonist-induce... | ACCEPT | Summary: Postsynaptic membrane (IEP). Reason: Location supported by synaptosome subfractionation and many other studies; accepted as for the other postsynaptic membrane rows. An expression-pattern code cannot establish a location, so the code is flagged upstream. 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 | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic membrane (ISO). Reason: GluA2-containing AMPARs act in the postsynaptic membrane of excitatory synapses (synaptic and perisynaptic). 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:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0045211 postsynaptic membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic membrane (ISO). Reason: GluA2-containing AMPARs act in the postsynaptic membrane of excitatory synapses (synaptic and perisynaptic). 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:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0045211 postsynaptic membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Postsynaptic membrane (ISS). Reason: GluA2-containing AMPARs act in the postsynaptic membrane of excitatory synapses (synaptic and perisynaptic). 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:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0045211 postsynaptic membrane | NAS PMID:17506699 The cell biology of synaptic plasticity: AMPA receptor traff... | ACCEPT | Summary: Postsynaptic membrane (NAS). Reason: GluA2-containing AMPARs act in the postsynaptic membrane of excitatory synapses (synaptic and perisynaptic). 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:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:11466413 PICK1 targets activated protein kinase Calpha to AMPA recept... | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm (IDA). Reason: Biosynthetic/intracellular pool of GluA2 in neurons and transfected cells; non-core. Supporting Evidence: PMID:11466413 PICK1-PKCalpha complexes are cotargeted with PICK1-GluR2 complexes to spines, where GluR2 is found to be phosphorylated by PKC on serine 880. |
| GO:0048787 presynaptic active zone membrane | IDA PMID:28057533 Presynaptic PICK1 facilitates trafficking of AMPA-receptors ... | KEEP AS NON CORE | Summary: Presynaptic active zone membrane (IDA). Reason: Immunogold EM shows GluA2 in the presynaptic active zone of Schaffer collateral synapses, regulated by PICK1 and NSF; real but secondary. Supporting Evidence: PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. |
| GO:0048787 presynaptic active zone membrane | IDA PMID:28057533 Presynaptic PICK1 facilitates trafficking of AMPA-receptors ... | KEEP AS NON CORE | Summary: Presynaptic active zone membrane (IDA). Reason: Immunogold EM shows GluA2 in the presynaptic active zone of Schaffer collateral synapses, regulated by PICK1 and NSF; real but secondary. Supporting Evidence: PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. |
| GO:0048787 presynaptic active zone membrane | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Presynaptic active zone membrane (IEA). Reason: Immunogold EM shows GluA2 in the presynaptic active zone of Schaffer collateral synapses, regulated by PICK1 and NSF; real but secondary. Supporting Evidence: PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. |
| GO:0050804 modulation of chemical synaptic transmission | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Modulation of chemical synaptic transmission (IBA). Reason: Regulated insertion and removal of GluA2-containing AMPARs is a principal way synaptic strength is modulated (LTP, LTD, scaling); kept as non-core beside the core transmission role. Supporting Evidence: PMID:17506699 The regulation of neurotransmitter receptors, such as the AMPA-type glutamate receptors (AMPARs), the major excitatory neurotransmitter receptors in the brain, is a crucial mechanism for the modulation of synaptic transmission. |
| 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: GluA2/3 continuous replacement maintains synaptic AMPAR number; GluA2 interactions with NSF and PDZ proteins sustain transmission. Non-core regulatory role. Supporting Evidence: PMID:11348590 GluR2/GluR3 receptors replace existing synaptic receptors continuously; this occurs only at synapses that already have AMPA-Rs and requires interactions by GluR2 with NSF and group II PDZ domain proteins. |
| GO:0051262 protein tetramerization | IDA PMID:19946266 X-ray structure, symmetry and mechanism of an AMPA-subtype g... | KEEP AS NON CORE | Summary: Protein tetramerization (IDA), structure of the GluA2 homotetramer. Reason: GluA2 self-assembles as a dimer of dimers into tetramers; this assembly step is required for channel function. Non-core. Supporting Evidence: PMID:19946266 Here we report the crystal structure of the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-sensitive, homotetrameric, rat GluA2 receptor at 3.6 A resolution in complex with a competitive antagonist. |
| GO:0051913 regulation of synaptic plasticity by chemical substance | IDA PMID:32071234 Tyrosine phosphorylation of the AMPA receptor subunit GluA2 ... | MODIFY | Summary: Regulation of synaptic plasticity by chemical substance (IDA), GluA2 Y876F knock-in mice and homeostatic scaling. Reason: The study shows GluA2 Tyr876 phosphorylation gates homeostatic upscaling (via GRIP1 recruitment); it is not about a chemical substance modulating plasticity. Lateral correction to GO:0150092 regulation of synaptic scaling. Proposed replacements: regulation of synaptic scaling Supporting Evidence: PMID:32071234 These results demonstrate that AMPAR trafficking during homeostatic upscaling can be gated by a single phosphorylation site on the GluA2 subunit. |
| GO:0051966 regulation of synaptic transmission, glutamatergic | IMP PMID:9697854 NSF binding to GluR2 regulates synaptic transmission. | KEEP AS NON CORE | Summary: Regulation of synaptic transmission, glutamatergic (IMP), NSF-binding peptide. Reason: Disrupting the GluA2-NSF interaction reduces AMPAR EPSCs, showing that GluA2 C-tail interactions maintain synaptic receptor levels. Non-core regulatory role. Supporting Evidence: PMID:9697854 Loading of decapeptides corresponding to the NSF-binding domain of GluR2 into rat hippocampal CA1 pyramidal neurons results in a marked, progressive decrement of AMPA receptor-mediated synaptic transmission. |
| GO:0060076 excitatory synapse | IDA PMID:10856222 Disruption of AMPA receptor GluR2 clusters following long-te... | KEEP AS NON CORE | Summary: Excitatory synapse (IDA). Reason: GluA2 clusters at excitatory synapses; glutamatergic synapse is the main term. Supporting Evidence: PMID:10856222 Moreover, GluR2 protein released from GRIP is shown to be internalized. |
| GO:0060078 regulation of postsynaptic membrane potential | IEA GO_REF:0000108 | ACCEPT | Summary: Regulation of postsynaptic membrane potential (IEA, from GO:1904315). Reason: GluA2-containing AMPARs depolarize the postsynaptic membrane upon glutamate binding. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. |
| GO:0060079 excitatory postsynaptic potential | IEA GO_REF:0000108 | ACCEPT | Summary: Excitatory postsynaptic potential (IEA). Reason: AMPAR currents carry the fast EPSP; consistent with the core function. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:9697854 Loading of decapeptides corresponding to the NSF-binding domain of GluR2 into rat hippocampal CA1 pyramidal neurons results in a marked, progressive decrement of AMPA receptor-mediated synaptic transmission. |
| GO:0060291 long-term synaptic potentiation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Long-term synaptic potentiation (IEA). Reason: LTP is expressed by insertion of AMPARs; GluA2 phosphorylation changes (S880 down, Y876 up) strengthen GRIP1 binding and AMPAR insertion during chemical LTP. GluA2-containing receptors carry the potentiated current, so this is a real but non-core role. Supporting Evidence: PMID:32948689 phosphorylation of serine-880 of the GluA2 AMPAR subunit (GluA2-S880) is decreased while phosphorylation of tyrosine-876 on GluA2 (GluA2-Y876) is elevated during chemically induced LTP. PMID:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0060291 long-term synaptic potentiation | IEP PMID:32948689 GRIP1 regulates synaptic plasticity and learning and memory. | KEEP AS NON CORE | Summary: Long-term synaptic potentiation (IEP). Reason: LTP is expressed by insertion of AMPARs; GluA2 phosphorylation changes (S880 down, Y876 up) strengthen GRIP1 binding and AMPAR insertion during chemical LTP. GluA2-containing receptors carry the potentiated current, so this is a real but non-core role. Supporting Evidence: PMID:32948689 phosphorylation of serine-880 of the GluA2 AMPAR subunit (GluA2-S880) is decreased while phosphorylation of tyrosine-876 on GluA2 (GluA2-Y876) is elevated during chemically induced LTP. PMID:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| GO:0060992 response to fungicide | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Response to fungicide (IEA), tributyltin decreases GluR2 expression. Reason: A reduction of GluA2 expression after toxicant exposure is a readout, not participation in a response to fungicide. Supporting Evidence: PMID:19591855 GluR2 protein was also reduced by long-term exposure to TBT. |
| 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 (IEP), tributyltin decreases GluR2 expression. Reason: A reduction of GluA2 expression after toxicant exposure is a readout, not participation in a response to fungicide. Supporting Evidence: PMID:19591855 GluR2 protein was also reduced by long-term exposure to TBT. |
| GO:0061846 dendritic spine cytoplasm | IDA PMID:28057533 Presynaptic PICK1 facilitates trafficking of AMPA-receptors ... | KEEP AS NON CORE | Summary: Dendritic spine cytoplasm (IDA). Reason: Intracellular (vesicular) GluA2 pools in spines; non-core. Supporting Evidence: PMID:17207780 Analyses revealed that the cytoplasmic pool of GluR2 receptors was twice as large compared to the GluR3, NR1, and NR2B subunits. |
| 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 increases surface GluR2. Reason: GluA2 surface levels change as a readout of dopamine treatment; GluA2 does not execute the response. Supporting Evidence: PMID:19674091 Repeated dopamine (DA) treatment, which leads to upregulation of surface GluR1 and GluR2, occluded activity blockade-induced synaptic scaling. |
| GO:0097060 synaptic membrane | IDA PMID:25129673 Impact of combined prenatal ethanol and prenatal stress expo... | KEEP AS NON CORE | Summary: Synaptic membrane (IDA), synaptosomal GluA2 levels. Reason: Synaptosomal fractions contain pre- and postsynaptic membranes; consistent with synaptic membrane localization. Non-core restatement of the postsynaptic membrane location. Supporting Evidence: PMID:25129673 TTTC significantly elevated both synaptosomal GluA1 and GluA2 subunit expression relative to the UPC group in control offspring |
| GO:0097060 synaptic membrane | IDA PMID:29134962 Role of Glutamatergic Projections from the Ventral CA1 to In... | KEEP AS NON CORE | Summary: Synaptic membrane (IDA), synaptosomal GluA2 levels. Reason: Synaptosomal fractions contain pre- and postsynaptic membranes; consistent with synaptic membrane localization. Non-core restatement of the postsynaptic membrane location. Supporting Evidence: PMID:29134962 decreased synaptosomal GluA2 expression in the IL |
| GO:0097060 synaptic membrane | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Synaptic membrane (ISO). Reason: Consistent with rat IDA rows; non-core. 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:10414981 Association of AMPA receptors with a subset of glutamate rec... | KEEP AS NON CORE | Summary: Scaffold protein binding (IPI, With PSD-95), GRIP/AMPAR association in brain. Reason: GluA2 directly binds scaffold proteins GRIP1/ABP and PICK1 through its PDZ ligand; the PSD-95 association is likely indirect (via TARPs). The specific mechanism is PDZ domain binding (accepted). Supporting Evidence: PMID:10414981 A majority of detergent-extractable GluR2/3 was complexed with GRIP in the brain. PMID:9768844 ABP binds to the GluR2/3 C-terminal VKI-COOH motif via class II hydrophobic PDZ interactions |
| GO:0097113 AMPA glutamate receptor clustering | IMP PMID:9069286 GRIP: a synaptic PDZ domain-containing protein that interact... | KEEP AS NON CORE | Summary: AMPA glutamate receptor clustering (IMP). Reason: GluA2 C-terminal binding to GRIP is required for AMPAR clustering; GluA2 contributes the binding motif that the scaffold clusters. Non-core trafficking role. Supporting Evidence: PMID:9069286 may be critical for the clustering of AMPA receptors at excitatory synapses in the brain. PMID:11931740 Dominant-negative constructs that interfere with the GRIP-liprin interaction disrupt the surface expression and dendritic clustering of AMPA receptors in cultured neurons. |
| GO:0098655 monoatomic cation transmembrane transport | IEA GO_REF:0000108 | ACCEPT | Summary: Monoatomic cation transmembrane transport (IEA). Reason: GluA2-containing AMPARs conduct Na+ and K+ (and Ca2+ only when unedited or absent). Supporting Evidence: file:rat/Gria2/Gria2-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:0098685 Schaffer collateral - CA1 synapse | IDA PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | KEEP AS NON CORE | Summary: Schaffer collateral - CA1 synapse (IDA). Reason: GluA2-containing AMPARs mediate transmission at CA3-CA1 synapses; a specific anatomical instance of glutamatergic synapse, kept as non-core. Supporting Evidence: PMID:11348590 GluR2/GluR3 receptors replace existing synaptic receptors continuously; this occurs only at synapses that already have AMPA-Rs and requires interactions by GluR2 with NSF and group II PDZ domain proteins. |
| GO:0098685 Schaffer collateral - CA1 synapse | IDA PMID:28057533 Presynaptic PICK1 facilitates trafficking of AMPA-receptors ... | KEEP AS NON CORE | Summary: Schaffer collateral - CA1 synapse (IDA). Reason: GluA2-containing AMPARs mediate transmission at CA3-CA1 synapses; a specific anatomical instance of glutamatergic synapse, kept as non-core. Supporting Evidence: PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. |
| GO:0098685 Schaffer collateral - CA1 synapse | IMP PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | KEEP AS NON CORE | Summary: Schaffer collateral - CA1 synapse (IMP). Reason: Location supported by other rows; a mutant phenotype cannot establish a location, so the code is flagged upstream. Supporting Evidence: PMID:11348590 GluR2/GluR3 receptors replace existing synaptic receptors continuously; this occurs only at synapses that already have AMPA-Rs and requires interactions by GluR2 with NSF and group II PDZ domain proteins. |
| GO:0098685 Schaffer collateral - CA1 synapse | ISO GO_REF:0000121 | KEEP AS NON CORE | Summary: Schaffer collateral - CA1 synapse (ISO). Reason: GluA2-containing AMPARs mediate transmission at CA3-CA1 synapses; a specific anatomical instance of glutamatergic synapse, kept as non-core. Supporting Evidence: PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. |
| 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: GluA2-containing AMPARs mediate transmission at CA3-CA1 synapses; a specific anatomical instance of glutamatergic synapse, kept as non-core. Supporting Evidence: PMID:30872532 the principal AMPAR complex at hippocampal synapses |
| GO:0098793 presynapse | IDA PMID:21807099 mGluR and NMDAR activation internalize distinct populations ... | KEEP AS NON CORE | Summary: Presynapse (IDA). Reason: GluA2 does occur presynaptically at some synapses (vesicles, active zone), so the term is kept as for the other presynaptic rows. Full text of the cited study read: it used synapsin only as a presynaptic marker to identify synaptic surface GluA2 puncta and did not localize GluA2 to the presynapse. Supporting Evidence: PMID:28057533 we demonstrate the association of AMPA receptors with the presynaptic active zone and with small presynaptic vesicles, in Schaffer collateral synapses in CA1 of the hippocampus. PMID:21807099 we immunolabeled surface GluA2s and the presynaptic marker synapsin in control and agonist treated neurons. |
| GO:0098839 postsynaptic density membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Postsynaptic density membrane (IBA). Reason: Core location: GluA2-containing AMPARs are anchored in the PSD membrane of excitatory synapses. Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. file:rat/Gria2/Gria2-uniprot.txt Postsynaptic density membrane |
| GO:0098839 postsynaptic density membrane | IDA PMID:28057533 Presynaptic PICK1 facilitates trafficking of AMPA-receptors ... | ACCEPT | Summary: Postsynaptic density membrane (IDA). Reason: Core location: GluA2-containing AMPARs are anchored in the PSD membrane of excitatory synapses. Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. file:rat/Gria2/Gria2-uniprot.txt Postsynaptic density membrane |
| GO:0098839 postsynaptic density membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Postsynaptic density membrane (IEA). Reason: Core location: GluA2-containing AMPARs are anchored in the PSD membrane of excitatory synapses. Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. file:rat/Gria2/Gria2-uniprot.txt Postsynaptic density membrane |
| GO:0098839 postsynaptic density membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic density membrane (ISO). Reason: Core location: GluA2-containing AMPARs are anchored in the PSD membrane of excitatory synapses. Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. file:rat/Gria2/Gria2-uniprot.txt Postsynaptic density membrane |
| GO:0098839 postsynaptic density membrane | ISO GO_REF:0000121 | ACCEPT | Summary: Postsynaptic density membrane (ISO). Reason: Core location: GluA2-containing AMPARs are anchored in the PSD membrane of excitatory synapses. Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. file:rat/Gria2/Gria2-uniprot.txt Postsynaptic density membrane |
| GO:0098839 postsynaptic density membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Postsynaptic density membrane (ISS). Reason: Core location: GluA2-containing AMPARs are anchored in the PSD membrane of excitatory synapses. Supporting Evidence: PMID:10701825 Ultrastructural studies have demonstrated that the glutamate receptor subunit proteins (e.g., GluR2) are frequently preferentially located at the postsynaptic density of asymmetric synapses. file:rat/Gria2/Gria2-uniprot.txt Postsynaptic density membrane |
| GO:0098978 glutamatergic synapse | IDA PMID:15610164 Presynaptic localization of an AMPA-type glutamate receptor ... | ACCEPT | Summary: Glutamatergic synapse (IDA). Reason: GluA2 functions at glutamatergic synapses as an AMPA receptor subunit. Supporting Evidence: PMID:10027300 In neurons, PICK1 specifically colocalizes with AMPA receptors at excitatory synapses. 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 (IEA). Reason: GluA2 functions at glutamatergic synapses as an AMPA receptor subunit. Supporting Evidence: PMID:10027300 In neurons, PICK1 specifically colocalizes with AMPA receptors at excitatory synapses. 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 | ISO GO_REF:0000121 | ACCEPT | Summary: Glutamatergic synapse (ISO). Reason: GluA2 functions at glutamatergic synapses as an AMPA receptor subunit. Supporting Evidence: PMID:10027300 In neurons, PICK1 specifically colocalizes with AMPA receptors at excitatory synapses. 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:0099094 ligand-gated monoatomic cation channel activity | IDA PMID:11773314 Voltage and concentration dependence of Ca(2+) permeability ... | ACCEPT | Summary: Ligand-gated monoatomic cation channel activity (IDA). Reason: Full text read: the study measured cation (Na+/Ca2+) permeation through glutamate-gated AMPA channels including GluR-B constructs. GluA2 forms a cation-selective ligand-gated channel; this term is in a branch parallel to GO:0004971 and is kept. Supporting Evidence: PMID:11773314 than that in unedited GluR-B(Q) channels file:rat/Gria2/Gria2-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:0099505 regulation of presynaptic membrane potential | IEA GO_REF:0000108 | MARK AS OVER ANNOTATED | Summary: Regulation of presynaptic membrane potential (IEA, from GO:0099507). Reason: Derived from SynGO rows whose cited paper has no presynaptic data. Presynaptic GluA2 exists at some terminals, but evidence that GluA2 regulates presynaptic membrane potential is not established. Supporting Evidence: PMID:10704491 we expressed the unedited form of GluR2 (GluR2Q) in oocytes, which produced large current responses sufficient for analysis of the kinetic properties. |
| GO:0099507 ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential | IDA PMID:10704491 Regulation of kinetic properties of GluR2 AMPA receptor chan... | MODIFY | Summary: Ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential (IDA). Reason: Full text read: the paper measures flip/flop desensitization kinetics of homomeric GluR2 in Xenopus oocytes; it has no presynaptic data. The channel activity is shown; the presynaptic context is not. Replace with GO:0004971 AMPA glutamate receptor activity and drop the context. Proposed replacements: AMPA glutamate receptor activity Context of precomposed term: context dropped Supporting Evidence: PMID:10704491 we expressed the unedited form of GluR2 (GluR2Q) in oocytes, which produced large current responses sufficient for analysis of the kinetic properties. |
| GO:0099507 ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential | IMP PMID:10704491 Regulation of kinetic properties of GluR2 AMPA receptor chan... | MODIFY | Summary: Ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential (IMP). Reason: Full text read: the paper measures flip/flop desensitization kinetics of homomeric GluR2 in Xenopus oocytes; it has no presynaptic data. The channel activity is shown; the presynaptic context is not. Replace with GO:0004971 AMPA glutamate receptor activity and drop the context. Proposed replacements: AMPA glutamate receptor activity Context of precomposed term: context dropped Supporting Evidence: PMID:10704491 we expressed the unedited form of GluR2 (GluR2Q) in oocytes, which produced large current responses sufficient for analysis of the kinetic properties. |
| GO:0099507 ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential | NAS PMID:10704491 Regulation of kinetic properties of GluR2 AMPA receptor chan... | MODIFY | Summary: Ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential (NAS). Reason: Full text read: the paper measures flip/flop desensitization kinetics of homomeric GluR2 in Xenopus oocytes; it has no presynaptic data. The channel activity is shown; the presynaptic context is not. Replace with GO:0004971 AMPA glutamate receptor activity and drop the context. Proposed replacements: AMPA glutamate receptor activity Context of precomposed term: context dropped Supporting Evidence: PMID:10704491 we expressed the unedited form of GluR2 (GluR2Q) in oocytes, which produced large current responses sufficient for analysis of the kinetic properties. |
| GO:0099544 perisynaptic space | ISO GO_REF:0000121 | MARK AS OVER ANNOTATED | Summary: Perisynaptic space (ISO from mouse Gria2). Reason: Perisynaptic space is extracellular region next to a synapse. GluA2 is an integral membrane protein found in perisynaptic membrane, not in the extracellular space. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: COMPARTMENT OR COMPLEX MISMATCH Sources checked: MGI:MGI:95809 SOURCE WEAK OR INFERRED Mouse source probably records perisynaptic membrane localization; the extracellular-space term does not fit a transmembrane receptor. Supporting Evidence: file:rat/Gria2/Gria2-uniprot.txt Postsynaptic density membrane |
| GO:0106033 spine synapse | IDA PMID:11007883 Phosphorylation of the AMPA receptor subunit GluR2 different... | KEEP AS NON CORE | Summary: Spine synapse (IDA). Reason: GluA2 at spine synapses; valid, non-core beside glutamatergic synapse. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:1900452 regulation of long-term synaptic depression | IDA PMID:10856222 Disruption of AMPA receptor GluR2 clusters following long-te... | KEEP AS NON CORE | Summary: Regulation of long-term synaptic depression (IDA). Reason: LTD is expressed by regulated endocytosis of GluA2-containing AMPARs, which depends on GluA2 C-tail motifs (Ser880 phosphorylation, the Tyr-rich 3Y region blocked by GluA2-3Y peptide). A real but non-core role of the trafficking tail. Supporting Evidence: PMID:10856222 stimulations inducing cerebellar LTD cause phosphorylation of Ser880 in the intracellular C-terminal domain of the AMPA receptor subunit GluR2. |
| GO:1900452 regulation of long-term synaptic depression | IMP PMID:16311338 Nucleus accumbens long-term depression and the expression of... | KEEP AS NON CORE | Summary: Regulation of long-term synaptic depression (IMP). Reason: LTD is expressed by regulated endocytosis of GluA2-containing AMPARs, which depends on GluA2 C-tail motifs (Ser880 phosphorylation, the Tyr-rich 3Y region blocked by GluA2-3Y peptide). A real but non-core role of the trafficking tail. Supporting Evidence: PMID:16311338 NAc LTD was blocked by a dynamin-derived peptide that inhibited clathrin-mediated endocytosis or by a GluR2-derived peptide that blocked regulated AMPAR endocytosis. |
| GO:1900452 regulation of long-term synaptic depression | IMP PMID:21187978 Synaptic neurotransmission depression in ventral tegmental d... | KEEP AS NON CORE | Summary: Regulation of long-term synaptic depression (IMP). Reason: LTD is expressed by regulated endocytosis of GluA2-containing AMPARs, which depends on GluA2 C-tail motifs (Ser880 phosphorylation, the Tyr-rich 3Y region blocked by GluA2-3Y peptide). A real but non-core role of the trafficking tail. Supporting Evidence: PMID:21187978 A GluR2-derived peptide blocks cannabinoid-induced VTA synaptic depression and conditioned place preference |
| GO:1900452 regulation of long-term synaptic depression | IMP PMID:37190555 Intravenous Injection of GluR2-3Y Inhibits Repeated Morphine... | KEEP AS NON CORE | Summary: Regulation of long-term synaptic depression (IMP). Reason: LTD is expressed by regulated endocytosis of GluA2-containing AMPARs, which depends on GluA2 C-tail motifs (Ser880 phosphorylation, the Tyr-rich 3Y region blocked by GluA2-3Y peptide). A real but non-core role of the trafficking tail. Supporting Evidence: PMID:37190555 Pretreatment with GluR2-3Y altered the ability of LTD induction to the level of that in the naive group |
| 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 (IBA). Reason: Core activity in context: GluA2-containing AMPARs are the glutamate-gated channels that depolarize the postsynaptic membrane at excitatory synapses. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:19946266 function by opening a transmembrane ion channel upon binding of glutamate |
| GO:1904315 transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | IDA PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | ACCEPT | Summary: Transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential (IDA). Reason: Core activity in context: GluA2-containing AMPARs are the glutamate-gated channels that depolarize the postsynaptic membrane at excitatory synapses. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:19946266 function by opening a transmembrane ion channel upon binding of glutamate |
| GO:1904315 transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | IMP PMID:11348590 Subunit-specific rules governing AMPA receptor trafficking t... | ACCEPT | Summary: Transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential (IMP). Reason: Core activity in context: GluA2-containing AMPARs are the glutamate-gated channels that depolarize the postsynaptic membrane at excitatory synapses. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:19946266 function by opening a transmembrane ion channel upon binding of glutamate |
| 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 (ISO). Reason: Core activity in context: GluA2-containing AMPARs are the glutamate-gated channels that depolarize the postsynaptic membrane at excitatory synapses. Supporting Evidence: PMID:11348590 AMPA-type glutamate receptors (AMPA-Rs) mediate a majority of excitatory synaptic transmission in the brain. PMID:19946266 function by opening a transmembrane ion channel upon binding of glutamate |
| GO:1904627 response to phorbol 13-acetate 12-myristate | IDA PMID:10856222 Disruption of AMPA receptor GluR2 clusters following long-te... | MARK AS OVER ANNOTATED | Summary: Response to phorbol 13-acetate 12-myristate (IDA). Reason: PKC activation by phorbol ester phosphorylates GluA2 Ser880 and triggers its internalization; GluA2 is the substrate/readout, not the executor of a response to the drug. Supporting Evidence: PMID:11007883 the Ser880-phosphorylated GluR2 subunits are enriched and colocalized with PICK1 in the dendrites, with very little staining observed at excitatory synapses. |
| GO:1904627 response to phorbol 13-acetate 12-myristate | IDA PMID:11466413 PICK1 targets activated protein kinase Calpha to AMPA recept... | MARK AS OVER ANNOTATED | Summary: Response to phorbol 13-acetate 12-myristate (IDA). Reason: PKC activation by phorbol ester phosphorylates GluA2 Ser880 and triggers its internalization; GluA2 is the substrate/readout, not the executor of a response to the drug. Supporting Evidence: PMID:11466413 PICK1-PKCalpha complexes are cotargeted with PICK1-GluR2 complexes to spines, where GluR2 is found to be phosphorylated by PKC on serine 880. |
| GO:1905430 cellular response to glycine | IDA PMID:21847098 PIKE-mediated PI3-kinase activity is required for AMPA recep... | MARK AS OVER ANNOTATED | Summary: Cellular response to glycine (IDA). Reason: Glycine is used as a chemical LTP stimulus that activates NMDA receptors; GluA2 trafficking is the readout of that protocol, not a response to glycine executed by GluA2. Supporting Evidence: PMID:21847098 PIKE-L directly interacts with both GluA2 and GRIP1 and forms a tertiary complex upon glycine-induced NMDA receptor activation. |
| GO:1905430 cellular response to glycine | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: Cellular response to glycine (IEA). Reason: Glycine is used as a chemical LTP stimulus that activates NMDA receptors; GluA2 trafficking is the readout of that protocol, not a response to glycine executed by GluA2. Supporting Evidence: PMID:22915106 GluA2 is restricted from trafficking to the cell surface by a glycine-induced increase in PICK1-GluA2 binding on endosomal compartments. |
| 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 (IEP). Reason: Glycine is used as a chemical LTP stimulus that activates NMDA receptors; GluA2 trafficking is the readout of that protocol, not a response to glycine executed by GluA2. Supporting Evidence: PMID:22915106 GluA2 is restricted from trafficking to the cell surface by a glycine-induced increase in PICK1-GluA2 binding on endosomal compartments. |
| 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 (IEP). Reason: Glycine is used as a chemical LTP stimulus that activates NMDA receptors; GluA2 trafficking is the readout of that protocol, not a response to glycine executed by GluA2. Supporting Evidence: PMID:32948689 This enhances the strength of the GRIP1-AMPAR association and, subsequently, the insertion of AMPARs into the postsynaptic membrane. |
| 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 brain-derived neurotrophic factor stimulus (IDA). Reason: BDNF signalling changes GluA2 protein levels, scaffold association and surface expression; GluA2 is a downstream target of the TrkB pathway, not a participant in the response. 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 brain-derived neurotrophic factor stimulus (IDA). Reason: BDNF signalling changes GluA2 protein levels, scaffold association and surface expression; GluA2 is a downstream target of the TrkB pathway, not a participant in the response. Supporting Evidence: PMID:23460828 acute BDNF treatment upregulates the interactions between AMPAr subunits (GluR1 and GluR2) with their scaffold proteins SAP97 and GRIP1 |
| 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 brain-derived neurotrophic factor stimulus (IEP). Reason: BDNF signalling changes GluA2 protein levels, scaffold association and surface expression; GluA2 is a downstream target of the TrkB pathway, not a participant in the response. 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:1990708 conditioned place preference | IMP PMID:21187978 Synaptic neurotransmission depression in ventral tegmental d... | MARK AS OVER ANNOTATED | Summary: Conditioned place preference (IMP), GluR2-derived interfering peptide in VTA. Reason: A behavioural outcome of blocking GluA2 endocytosis; the peptide perturbs LTD at VTA synapses. GluA2 does not itself carry out place-preference learning. Supporting Evidence: PMID:21187978 A GluR2-derived peptide blocks cannabinoid-induced VTA synaptic depression and conditioned place preference |
| GO:2000463 positive regulation of excitatory postsynaptic potential | IMP PMID:9697854 NSF binding to GluR2 regulates synaptic transmission. | KEEP AS NON CORE | Summary: Positive regulation of excitatory postsynaptic potential (IMP), NSF-binding peptide. Reason: Blocking the GluA2-NSF interaction progressively reduces AMPAR EPSCs, showing GluA2 C-tail interactions sustain EPSP amplitude. Non-core regulatory role. Supporting Evidence: PMID:9697854 Loading of decapeptides corresponding to the NSF-binding domain of GluR2 into rat hippocampal CA1 pyramidal neurons results in a marked, progressive decrement of AMPA receptor-mediated synaptic transmission. |
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Download this section (compressed HTML)Q: Should GO:0022849 glutamate-gated calcium ion channel activity be restricted to GluA2-lacking AMPA receptors, given that native GluA2 is Q/R-edited and renders receptors Ca2+-impermeable, with Ca2+ permeability shown only for unedited or mutant GluA2 constructs?
Q: Is there direct evidence that presynaptic GluA2-containing receptors regulate presynaptic membrane potential or release, which would justify GO:0099507 for GluA2 from a suitable paper?
Experiment: Compare presynaptic release probability in terminal-specific Gria2 conditional knockouts at corticostriatal synapses, to test whether presynaptic GluA2-containing AMPARs regulate presynaptic membrane potential.
Hypothesis: Presynaptic GluA2-containing AMPA receptors depolarize corticostriatal terminals and modulate glutamate release.
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