ICA1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0030667 secretory granule membrane	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically-inferred annotation for secretory granule membrane localization. Strongly supported by experimental IDA evidence and consistent with ICA1's role in insulin granule biogenesis. Reason: IBA annotation is well-supported by direct experimental evidence (IDA from PMID:12682071) and consistent with the protein's established role in secretory granule biogenesis. The phylogenetic inference is robust given conservation of ICA1 function across species (C. elegans RIC-19, mouse Ica1). Supporting Evidence: PMID:12682071 Virtually no ICA69 immunogold labeling was observed on secretory granules near the plasma membrane, suggesting that ICA69 dissociates from secretory granule membranes during their maturation. file:human/ICA1/ICA1-uniprot.txt Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein. file:human/ICA1/ICA1-deep-research-falcon.md See deep research file for comprehensive analysis
GO:0051046 regulation of secretion	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically-inferred annotation for regulation of secretion. ICA1 regulates dense-core secretory vesicle biogenesis, essential for insulin and neurotransmitter secretion. Reason: This IBA annotation accurately captures ICA1's core biological function. Multiple lines of evidence support this - Ica1 knockout mice show impaired insulin granule maturation and elevated blood glucose, and ICA1-null mice have defective AMPA receptor insertion. The C. elegans homolog RIC-19 is required for neuropeptide secretion. This is a central, conserved function. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md ICA1 knockout mice show impaired insulin granule maturation, elevated blood glucose, increased proinsulin-to-insulin ratios. PICK1-deficient mice show complete loss of ICA1 protein. file:human/ICA1/ICA1-uniprot.txt May play a role in neurotransmitter secretion.
GO:0097753 membrane bending	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically-inferred annotation for membrane bending activity. ICA1 contains a BAR (Bin/Amphiphysin/Rvs) domain that induces membrane curvature during vesicle budding. Reason: This IBA annotation accurately represents the mechanistic function of ICA1's BAR domain. The BAR domain forms dimers that both sense and induce membrane curvature, which is essential for vesicle budding from the TGN. This function is conserved across the arfaptin-related protein family and is well-characterized for ICA1. Supporting Evidence: PMID:12682071 In silico sequence and structural analyses revealed that the N-terminal region of ICA69 is similar to the region of arfaptins that interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. file:human/ICA1/ICA1-uniprot.txt DOMAIN 51..254 AH [Arfaptin homology domain/BAR domain]
GO:0140090 membrane curvature sensor activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetically-inferred annotation for membrane curvature sensor activity. This is the primary molecular function of ICA1's BAR domain, confirmed by direct experimental evidence. Reason: This IBA annotation is particularly well-supported. PMID:29768204 directly demonstrates that ICA1 (and homologs PICK1 and arfaptin2) possess membrane curvature sensing activity mediated by an amphipathic helix N-terminal to the BAR domain. The study shows that disrupting this helix impairs curvature sensing and compromises ICA1 localization to high-curvature insulin granules. This is ICA1's core molecular function. Supporting Evidence: PMID:29768204 Here, we show that membrane curvature sensing (MCS) directs cellular localization and function of the BAR domain protein PICK1. In PICK1, and the homologous proteins ICA69 and arfaptin2, we identify an amphipathic helix N-terminal to the BAR domain that mediates MCS. Mutational disruption of the helix in PICK1 impaired MCS without affecting membrane binding per se. file:human/ICA1/ICA1-uniprot.txt DOMAIN 51..254 AH [Arfaptin homology domain/BAR domain]
GO:0000139 Golgi membrane	IEA GO_REF:0000044	ACCEPT	Summary: Automated annotation based on UniProt subcellular location vocabulary. ICA1 is a peripheral membrane protein at the Golgi complex, supported by direct experimental evidence. Reason: While this is an IEA (electronically inferred) annotation, it is well-supported by experimental evidence (IDA from PMID:12682071). The Golgi membrane is a primary site of ICA1 function where it regulates vesicle budding from the TGN. The automated mapping from UniProt is accurate. Supporting Evidence: PMID:12682071 Confocal microscopy and subcellular fractionation in INS-1 cells showed co-localization of ICA69 with markers of the Golgi complex and, to a minor extent, with immature insulin-containing secretory granules file:human/ICA1/ICA1-uniprot.txt Golgi apparatus membrane; Peripheral membrane protein.
GO:0005737 cytoplasm	IEA GO_REF:0000117	ACCEPT	Summary: Automated annotation by ARBA machine learning model. ICA1 is predominantly cytoplasmic/cytosolic with dynamic membrane association. Redundant with TAS annotation. Reason: Accurate automated annotation. ICA1 is primarily cytoplasmic, supported by multiple experimental annotations (TAS from PMID:8326004, IDA from HPA). The ARBA machine learning prediction correctly identifies this localization. While redundant with other annotations, it demonstrates robust automated curation. Supporting Evidence: PMID:8326004 Islet cell autoantigen 69 kD (ICA69) file:human/ICA1/ICA1-uniprot.txt Predominantly cytosolic.
GO:0005829 cytosol	IEA GO_REF:0000120	ACCEPT	Summary: Automated annotation based on combined IEA methods including orthology to mouse Ica1 (P97411). Redundant with IDA and ISS annotations but accurate. Reason: Accurate automated annotation inferred from mouse ortholog localization. ICA1 is predominantly cytosolic as confirmed by multiple experimental sources (IDA from HPA, ISS from mouse). While redundant, this demonstrates consistent orthology-based inference. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt Cytoplasm, cytosol. Predominantly cytosolic.
GO:0006836 neurotransmitter transport	IEA GO_REF:0000043	ACCEPT	Summary: Automated annotation from UniProt keyword mapping. ICA1 regulates dense-core vesicle biogenesis in neurons, affecting AMPA receptor trafficking and synaptic transmission. Reason: This automated annotation based on the "Neurotransmitter transport" keyword is accurate but somewhat indirect. ICA1 doesn't directly transport neurotransmitters, but it regulates the biogenesis of dense-core vesicles that contain neurotransmitters and controls AMPA receptor delivery to synapses. The C. elegans homolog RIC-19 is required for neuropeptide secretion, supporting this functional annotation. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt May play a role in neurotransmitter secretion. file:human/ICA1/ICA1-deep-research-openai.md In neurons, ICA1-PICK1 complexes control AMPA receptor (AMPAR) delivery to synapses. ICA1-null mice have normal basal synaptic transmission but selective impairment in long-term potentiation (LTP).
GO:0012505 endomembrane system	IEA GO_REF:0000117	ACCEPT	Summary: Automated ARBA annotation for endomembrane system localization. ICA1 functions at multiple endomembrane compartments including Golgi, TGN, and secretory vesicles. Reason: Accurate broad annotation from ARBA machine learning. ICA1 functions within the endomembrane system, specifically at the Golgi/TGN and associated vesicles in the secretory pathway. This is a general term that encompasses ICA1's more specific localizations (Golgi membrane, secretory granule membrane). Appropriately broad for automated annotation. Supporting Evidence: PMID:12682071 ICA69 is therefore a novel arfaptin-related protein that is likely to play a role in membrane trafficking at the Golgi complex and immature secretory granules in neurosecretory cells. file:human/ICA1/ICA1-uniprot.txt Golgi apparatus membrane; Cytoplasmic vesicle, secretory vesicle membrane
GO:0019904 protein domain specific binding	IEA GO_REF:0000002	ACCEPT	Summary: Automated annotation from InterPro domain IPR010504 (Arfaptin homology domain). ICA1's BAR/AH domain mediates protein-protein interactions with PICK1, Rab2, and membrane components. Reason: Accurate automated annotation. The InterPro mapping correctly identifies that ICA1's arfaptin homology (AH) domain mediates protein domain-specific binding. ICA1 forms heterodimers with PICK1 through BAR domain interactions and binds Rab2 GTPases. While "protein domain specific binding" is more informative than generic "protein binding", it could still be more specific. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt DOMAIN 51..254 AH [Arfaptin homology domain/BAR domain]. Q05084; P61019: RAB2A; NbExp=4 file:human/ICA1/ICA1-deep-research-openai.md Forms stable heterodimers with PICK1 (Protein Interacting with C Kinase 1), another BAR domain protein.
GO:0030658 transport vesicle membrane	IEA GO_REF:0000044	ACCEPT	Summary: Automated annotation from UniProt subcellular location mapping. ICA1 localizes to transport vesicles (secretory granules) budding from the Golgi/TGN. Reason: Accurate automated annotation. ICA1 associates with the membranes of transport vesicles, specifically immature secretory granules that are transport vesicles carrying cargo from the TGN to the cell periphery. This is supported by immunoelectron microscopy data showing ICA1 on vesicles. Supporting Evidence: PMID:12682071 The association of ICA69 with these organelles was confirmed by immunoelectron microscopy. [...] ICA69 dissociates from secretory granule membranes during their maturation. file:human/ICA1/ICA1-uniprot.txt Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein.
GO:0030672 synaptic vesicle membrane	IEA GO_REF:0000120	ACCEPT	Summary: Automated annotation from combined IEA methods and mouse ortholog. ICA1 regulates dense-core vesicle biogenesis in neurons, with documented synaptic function in AMPA receptor trafficking. Reason: Accurate automated annotation supported by experimental data. While ICA1's primary characterized role in neurons involves AMPA receptor trafficking rather than classical synaptic vesicle function, it does associate with vesicle membranes in neurons and the deep research indicates involvement in synaptic processes. The ISS annotation from mouse supports this. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein. file:human/ICA1/ICA1-deep-research-openai.md In neurons, ICA1-PICK1 complexes control AMPA receptor (AMPAR) delivery to synapses. [...] Functions in de novo secretory pathway for AMPARs from Golgi to synaptic membrane.
GO:0031410 cytoplasmic vesicle	IEA GO_REF:0000043	ACCEPT	Summary: Automated annotation from UniProt keyword mapping. Broad cellular component term encompassing ICA1's localization to secretory granules and synaptic vesicles. Reason: Accurate but broad automated annotation. ICA1 localizes to various cytoplasmic vesicles, including secretory granules and synaptic vesicles. This general term is appropriate as a parent of the more specific vesicle membrane annotations. Supported by experimental evidence for specific vesicle types. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt Also exists as a membrane-bound form which has been found associated with synaptic vesicles and also with the Golgi complex and immature secretory granules. file:human/ICA1/ICA1-uniprot.txt Cytoplasmic vesicle, secretory vesicle membrane
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MODIFY	Summary: Proteome-scale interactome mapping identifying ICA1 interactions including RAB2A, RAB2B, MBD3, ING5, and CCDC28A. While accurate, the term "protein binding" is uninformative for a scaffolding protein. Reason: The generic "protein binding" term does not capture the functional significance of ICA1 as a scaffolding protein and Rab2 effector. ICA1's interactions are central to its role in vesicle trafficking, forming PICK1-ICA1 heterodimers and binding Rab2 GTPases. More specific molecular function terms would better represent this activity. Proposed replacements: protein-macromolecule adaptor activity protein-membrane adaptor activity Supporting Evidence: PMID:25416956 Here, we describe a systematic map of ?14,000 high-quality human binary protein-protein interactions file:human/ICA1/ICA1-uniprot.txt Q05084; P61019: RAB2A; NbExp=4; IntAct=EBI-1046751, EBI-752037; Q05084; Q8WUD1: RAB2B; NbExp=4
GO:0005515 protein binding	IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m...	MODIFY	Summary: High-throughput interactome study identifying ICA1 protein-protein interactions with RAB2A and RAB2B. While technically correct, "protein binding" is uninformative. Reason: The term "protein binding" lacks specificity and does not convey the functional significance of ICA1's interactions. ICA1 functions as a scaffolding protein and Rab2 effector. Should be replaced with more informative molecular function terms that capture its adapter/scaffolding role in vesicle trafficking. Proposed replacements: protein-macromolecule adaptor activity protein-membrane adaptor activity Supporting Evidence: PMID:29892012 Large-scale studies of known disease-associated mutations have already reported a strong association with binding interfaces of protein interactions 23 , 24
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: Cytosol localization based on immunofluorescence data from Human Protein Atlas. ICA1 is predominantly cytosolic with dynamic membrane association. Reason: Confirmed by multiple lines of evidence. UniProt states "Predominantly cytosolic" and this is consistent with the protein's function as a cytosolic adaptor that transiently associates with membranes during vesicle biogenesis. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt Predominantly cytosolic. Also exists as a membrane-bound form which has been found associated with synaptic vesicles and also with the Golgi complex and immature secretory granules.
GO:0140090 membrane curvature sensor activity	IDA PMID:29768204 An Amphipathic Helix Directs Cellular Membrane Curvature Sen...	ACCEPT	Summary: Direct experimental demonstration (IDA) from Herlo et al. (2018) showing that ICA1, along with PICK1 and arfaptin2, possesses membrane curvature sensing activity mediated by an amphipathic helix. Reason: Excellent direct experimental evidence. This paper specifically demonstrates membrane curvature sensing for ICA1 (ICA69) using super-resolution microscopy in insulin-producing cells, showing size-dependent binding on insulin granules. Mutational disruption of the amphipathic helix impaired curvature sensing without affecting membrane binding. This is ICA1's primary molecular function and this annotation is strongly supported. Supporting Evidence: PMID:29768204 In PICK1, and the homologous proteins ICA69 and arfaptin2, we identify an amphipathic helix N-terminal to the BAR domain that mediates MCS. Mutational disruption of the helix in PICK1 impaired MCS without affecting membrane binding per se. In insulin-producing INS-1E cells, super-resolution microscopy revealed that disruption of the helix selectively compromised PICK1 density on insulin granules of high curvature during their maturation.
GO:0005829 cytosol	ISS GO_REF:0000024	ACCEPT	Summary: Cytosol localization inferred from mouse ortholog (P97411). Redundant with experimental IDA annotation but supports conservation. Reason: Sequence similarity-based annotation from mouse ortholog. While redundant with the IDA annotation, it confirms evolutionary conservation of subcellular localization. The ISS annotation is appropriately conservative. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt Predominantly cytosolic.
GO:0030672 synaptic vesicle membrane	ISS GO_REF:0000024	ACCEPT	Summary: Manual transfer from mouse ortholog (P97411) based on sequence similarity. ICA1 associates with synaptic vesicle membranes in neurons, supported by UniProt annotation. Reason: Appropriately conservative ISS annotation based on mouse ortholog. The manual curator judgment of sequence similarity is sound given the high conservation between human and mouse ICA1. While the primary neuronal function involves AMPA receptor trafficking, the protein does associate with synaptic vesicle membranes. Supported by UniProt subcellular location data. Supporting Evidence: file:human/ICA1/ICA1-uniprot.txt Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein. Also exists as a membrane-bound form which has been found associated with synaptic vesicles.
GO:0000139 Golgi membrane	IDA PMID:12682071 Islet cell autoantigen of 69 kDa is an arfaptin-related prot...	ACCEPT	Summary: Direct experimental evidence from Spitzenberger et al. (2003) showing ICA1 enrichment in perinuclear region and co-localization with Golgi markers in insulinoma INS-1 cells by confocal microscopy and subcellular fractionation. Reason: Strong experimental support. The paper demonstrates by confocal microscopy, subcellular fractionation, and immunoelectron microscopy that ICA1 localizes to the Golgi complex in insulinoma cells. This is a core site of function where ICA1 regulates vesicle budding from the trans-Golgi network. Supporting Evidence: PMID:12682071 Confocal microscopy and subcellular fractionation in INS-1 cells showed co-localization of ICA69 with markers of the Golgi complex and, to a minor extent, with immature insulin-containing secretory granules. file:human/ICA1/ICA1-uniprot.txt Golgi apparatus membrane; Peripheral membrane protein.
GO:0030667 secretory granule membrane	IDA PMID:12682071 Islet cell autoantigen of 69 kDa is an arfaptin-related prot...	ACCEPT	Summary: Direct experimental evidence from Spitzenberger et al. (2003) showing ICA1 association with immature insulin-containing secretory granules. Immunoelectron microscopy showed ICA1 dissociates from granules during maturation. Reason: Strong experimental support from the same paper. The immunoelectron microscopy data specifically shows ICA1 on immature secretory granules budding from TGN, with virtually no labeling on mature granules near plasma membrane. This dynamic localization is central to ICA1's function in granule biogenesis and maturation. Supporting Evidence: PMID:12682071 Confocal microscopy and subcellular fractionation in INS-1 cells showed co-localization of ICA69 with markers of the Golgi complex and, to a minor extent, with immature insulin-containing secretory granules. [...] Virtually no ICA69 immunogold labeling was observed on secretory granules near the plasma membrane, suggesting that ICA69 dissociates from secretory granule membranes during their maturation. file:human/ICA1/ICA1-uniprot.txt Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein.
GO:0005737 cytoplasm	TAS PMID:8326004 Islet cell autoantigen 69 kD (ICA69). Molecular cloning and ...	ACCEPT	Summary: Traceable author statement from original ICA1 discovery paper (Pietropaolo et al. 1993) describing ICA69 as a cytosolic protein. This was the first molecular characterization of the protein. Reason: Historical annotation from the original gene characterization paper. While subsequent work has refined understanding of its dynamic membrane association, the cytoplasmic/cytosolic localization is accurate. TAS (Traceable Author Statement) is appropriate evidence code for this foundational paper. Supporting Evidence: PMID:8326004 Islet cell autoantigen 69 kD (ICA69) file:human/ICA1/ICA1-uniprot.txt Predominantly cytosolic.
GO:0032127 dense core granule membrane	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md Forms stable heterodimers with PICK1 (Protein Interacting with C Kinase 1), another BAR domain protein. PICK1-ICA1 complexes bind immature insulin granules budding from trans-Golgi network (TGN), orchestrating granule formation and maturation. ICA1 dissociates once granules mature. file:human/ICA1/ICA1-deep-research-openai.md Ica1 knockout mice show impaired insulin granule maturation, elevated blood glucose, increased proinsulin-to-insulin ratios. PICK1-deficient mice show complete loss of ICA1 protein, indicating interdependence.
GO:1990502 dense core granule maturation	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md Forms stable heterodimers with PICK1 (Protein Interacting with C Kinase 1), another BAR domain protein. PICK1-ICA1 complexes bind immature insulin granules budding from trans-Golgi network (TGN), orchestrating granule formation and maturation. ICA1 dissociates once granules mature. file:human/ICA1/ICA1-deep-research-openai.md Ica1 knockout mice show impaired insulin granule maturation, elevated blood glucose, increased proinsulin-to-insulin ratios. PICK1-deficient mice show complete loss of ICA1 protein, indicating interdependence.
GO:0033363 secretory granule organization	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: PMID:29768204 In PICK1, and the homologous proteins ICA69 and arfaptin2, we identify an amphipathic helix N-terminal to the BAR domain that mediates MCS. Mutational disruption of the helix in PICK1 impaired MCS without affecting membrane binding per se. In insulin-producing INS-1E cells, super-resolution microscopy revealed that disruption of the helix selectively compromised PICK1 density on insulin granules of high curvature during their maturation. PMID:12682071 ICA69 is therefore a novel arfaptin-related protein that is likely to play a role in membrane trafficking at the Golgi complex and immature secretory granules in neurosecretory cells.
GO:0030073 insulin secretion	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md Forms stable heterodimers with PICK1 (Protein Interacting with C Kinase 1), another BAR domain protein. PICK1-ICA1 complexes bind immature insulin granules budding from trans-Golgi network (TGN), orchestrating granule formation and maturation. ICA1 dissociates once granules mature. file:human/ICA1/ICA1-deep-research-openai.md Ica1 knockout mice show impaired insulin granule maturation, elevated blood glucose, increased proinsulin-to-insulin ratios. PICK1-deficient mice show complete loss of ICA1 protein, indicating interdependence.
GO:0045211 postsynaptic membrane	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md In neurons, ICA1-PICK1 complexes control AMPA receptor (AMPAR) delivery to synapses. ICA1-null mice have normal basal synaptic transmission but selective impairment in long-term potentiation (LTP) - activity-dependent AMPAR insertion during LTP is defective, causing hippocampus-dependent learning deficits. file:human/ICA1/ICA1-deep-research-openai.md ICA1 stabilizes PICK1 localization in neurons. Functions in de novo secretory pathway for AMPARs from Golgi to synaptic membrane.
GO:0098970 postsynaptic neurotransmitter receptor diffusion trapping	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md In neurons, ICA1-PICK1 complexes control AMPA receptor (AMPAR) delivery to synapses. ICA1-null mice have normal basal synaptic transmission but selective impairment in long-term potentiation (LTP) - activity-dependent AMPAR insertion during LTP is defective, causing hippocampus-dependent learning deficits. file:human/ICA1/ICA1-deep-research-openai.md ICA1 stabilizes PICK1 localization in neurons. Functions in de novo secretory pathway for AMPARs from Golgi to synaptic membrane.
GO:0048167 regulation of synaptic plasticity	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md In neurons, ICA1-PICK1 complexes control AMPA receptor (AMPAR) delivery to synapses. ICA1-null mice have normal basal synaptic transmission but selective impairment in long-term potentiation (LTP) - activity-dependent AMPAR insertion during LTP is defective, causing hippocampus-dependent learning deficits. file:human/ICA1/ICA1-deep-research-openai.md ICA1 stabilizes PICK1 localization in neurons. Functions in de novo secretory pathway for AMPARs from Golgi to synaptic membrane.
GO:0099645 neurotransmitter receptor localization to postsynaptic specialization membrane	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations. Supporting Evidence: file:human/ICA1/ICA1-deep-research-openai.md In neurons, ICA1-PICK1 complexes control AMPA receptor (AMPAR) delivery to synapses. ICA1-null mice have normal basal synaptic transmission but selective impairment in long-term potentiation (LTP) - activity-dependent AMPAR insertion during LTP is defective, causing hippocampus-dependent learning deficits. file:human/ICA1/ICA1-deep-research-openai.md ICA1 stabilizes PICK1 localization in neurons. Functions in de novo secretory pathway for AMPARs from Golgi to synaptic membrane.

Gene Description

Existing Annotations Review

Core Functions

Sensing membrane curvature at trans-Golgi network to regulate dense-core granule budding and maturation

Scaffolding protein-membrane interactions to orchestrate insulin granule biogenesis in pancreatic beta cells

Regulating AMPA receptor trafficking from Golgi to synaptic membrane in neurons for activity-dependent synaptic plasticity

References

Deep Research

Cyberian

Falcon

OpenAI

📚 Additional Documentation

Notes

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