ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007
PICK1-ICA69 heteromeric BAR domain complex regulates synaptic targeting and surface expression of AMPA receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 79 citations in OpenAlex.
- PICK1 links KIBRA and AMPA receptor subunit GluA2 in coiled-coil-driven supramolecular complexes.The Journal of biological chemistry · 2025Article
- Utilizing AfDesign for Developing a Small Molecule Inhibitor of PICK- 1-PDZ.Current protein & peptide science · 2025Article
- Sodium arsenite induces aggresome formation by promoting PICK1 BAR domain homodimer formation.Molecular biology of the cell · 2024Article
- ICA1 affects APP processing through the PICK1-PKCα signaling pathway.CNS neuroscience & therapeutics · 2024Article
- PICK1-Deficient Mice Maintain Their Glucose Tolerance During Diet-Induced Obesity.Journal of the Endocrine Society · 2023Article
- Spinophilin-dependent regulation of GluN2B-containing NMDAR-dependent calcium influx, GluN2B surface expression, and cleaved caspase expression.Synapse (New York, N.Y.) · 2023Article
- Truncating PICK1 Variant Identified in Azoospermia Affected Mitochondrial Dysfunction in Knockout Mice.Current medical science · 2023Article
- ICA69 regulates activity-dependent synaptic strengthening and learning and memory.Frontiers in molecular neuroscience · 2023Article
- The adaptor protein PICK1 targets the sorting receptor SorLA.Molecular brain · 2022Article
- CaFrontiers in molecular neuroscience · 2022Article
- Revisiting I-BAR Proteins at Central Synapses.Frontiers in neural circuits · 2021Review
- A high-affinity, bivalent PDZ domain inhibitor complexes PICK1 to alleviate neuropathic pain.EMBO molecular medicine · 2020Article
- A genome-wide association study of tramadol metabolism from post-mortem samples.The pharmacogenomics journal · 2020Article
- AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking.Cellular and molecular life sciences : CMLS · 2019Review
- Neuroligins Differentially Mediate Subtype-Specific Synapse Formation in Pyramidal Neurons and Interneurons.Neuroscience bulletin · 2019Article
- Article
- BAR domain proteins-a linkage between cellular membranes, signaling pathways, and the actin cytoskeleton.Biophysical reviews · 2018Review
- Arc/Arg3.1 has an activity-regulated interaction with PICK1 that results in altered spatial dynamics.Scientific reports · 2018Article
- PICK1 inhibits the E3 ubiquitin ligase activity of Parkin and reduces its neuronal protective effect.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- PICK1 is essential for insulin production and the maintenance of glucose homeostasis.Molecular biology of the cell · 2018Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The trafficking of AMPA-type glutamate receptors to and from synapses is an important mechanism underlying synaptic plasticity, a cellular model of learning and memory. PICK1 (protein interacts with C-kinase 1) is a peripheral membrane protein that interacts with AMPA receptors and regulates their trafficking. PICK1 contains a PDZ (PSD-95/Dlg/ZO1) domain and a BAR (Bin/amphiphysin/Rvs) domain. The PDZ domain of PICK1 interacts with the intracellular C-terminal tails of AMPA receptors, while the BAR domain binds to lipid membranes. Both the AMPA receptor interaction and the lipid binding of PICK1 are important to AMPA receptor trafficking and synaptic plasticity. Here, we identified ICA69 (islet cell autoantigen 69 kDa), another BAR-domain-containing protein, as the major binding partner of PICK1. Over three-fourths of ICA69 and PICK1 associate with each other in the brain. The BAR domain of ICA69 also binds to liposomes and forms heteromeric BAR domain complexes with PICK1. ICA69 coexpresses with PICK1 in different tissues and at various developmental stages. In neurons, although ICA69 colocalizes well with PICK1 in cell bodies and dendrites, it is surprisingly absent from synapses, where PICK1 is enriched. Furthermore, overexpression of ICA69 redistributes PICK1 from synapses to dendrites. ICA69 also disrupts the PICK1-induced clustering of AMPA receptors and reduces synaptic targeting and surface expression of the receptors. ICA69 regulates AMPA receptor trafficking by forming heteromeric BAR domain complexes with PICK1 and preventing formation of PICK1 homomeric complexes. Together, our results suggest that the switch from ICA69-PICK1 heteromeric complexes to PICK1-PICK1 homomeric complexes could be an important mechanism regulating synaptic targeting and surface expression of AMPA receptors.
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