ArticleProceedings of the National Academy of Sciences of the United States of America2013
PICK1 interacts with PACSIN to regulate AMPA receptor internalization and cerebellar long-term depression.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 80 citations in OpenAlex.
- PACSIN2-mediated synaptic injury contributes to behavioral disorders caused by chronic stress.Acta pharmacologica Sinica · 2026Article
- SNX6-mediated subunit-specific secretory trafficking of AMPA receptors regulates synaptic function and plasticity.Communications biology · 2025Article
- Male caregiving experience alters hippocampal neuroplasticity and transcription independent of reproduction in a biparental species.Communications biology · 2025Article
- PICK1 links KIBRA and AMPA receptor subunit GluA2 in coiled-coil-driven supramolecular complexes.The Journal of biological chemistry · 2025Article
- Loss of the proton-activated chloride channel in neurons impairs AMPA receptor endocytosis and LTD via endosomal hyper-acidification.Cell reports · 2025Article
- Utilizing AfDesign for Developing a Small Molecule Inhibitor of PICK- 1-PDZ.Current protein & peptide science · 2025Article
- junctionCounts: comprehensive alternative splicing analysis and prediction of isoform-level impacts to the coding sequence.NAR genomics and bioinformatics · 2024Article
- PACSIN1 promotes immunosuppression in gastric cancer by degrading MHC-I.Acta biochimica et biophysica Sinica · 2024Article
- Tyro3 promotes the maturation of glutamatergic synapses.Frontiers in neuroscience · 2024Article
- Fluorescence lifetime imaging of AMPA receptor endocytosis in living neurons: effects of Aβ and PP1.Frontiers in molecular neuroscience · 2024Article
- Dysfunction of Glutamatergic Synaptic Transmission in Depression: Focus on AMPA Receptor Trafficking.Biological psychiatry global open science · 2023Review
- ICA69 regulates activity-dependent synaptic strengthening and learning and memory.Frontiers in molecular neuroscience · 2023Article
- Alterations in the Proteome of Developing Neocortical Synaptosomes in the Absence of MET Signaling Revealed by Comparative Proteomics.Developmental neuroscience · 2023Article
- Familial ALS-associatedOpen biology · 2022Article
- PACSIN1 is indispensable for amphisome-lysosome fusion during basal autophagy and subsets of selective autophagy.PLoS genetics · 2022Article
- PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022Review
- Syndapin-2 mediated transcytosis of amyloid-β across the blood-brain barrier.Brain communications · 2022Article
- Biological Significance of the Protein Changes Occurring in the Cerebrospinal Fluid of Alzheimer's Disease Patients: Getting Clues from Proteomic Studies.Diagnostics (Basel, Switzerland) · 2021Review
- Regulation of Synapse Weakening through Interactions of the Microtubule Associated Protein Tau with PACSIN1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Regulation of NMDA receptor trafficking and gating by activity-dependent CaMKIIα phosphorylation of the GluN2A subunit.Cell reports · 2021Article
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Authors and funding
11 authors at 5 institutions in 4 countries.
Funding
Abstract
The dynamic trafficking of AMPA receptors (AMPARs) into and out of synapses is crucial for synaptic transmission, plasticity, learning, and memory. The protein interacting with C-kinase 1 (PICK1) directly interacts with GluA2/3 subunits of the AMPARs. Although the role of PICK1 in regulating AMPAR trafficking and multiple forms of synaptic plasticity is known, the exact molecular mechanisms underlying this process remain unclear. Here, we report a unique interaction between PICK1 and all three members of the protein kinase C and casein kinase II substrate in neurons (PACSIN) family and show that they form a complex with AMPARs. Our results reveal that knockdown of the neuronal-specific protein, PACSIN1, leads to a significant reduction in AMPAR internalization following the activation of NMDA receptors in hippocampal neurons. The interaction between PICK1 and PACSIN1 is regulated by PACSIN1 phosphorylation within the variable region and is required for AMPAR endocytosis. Similarly, the binding of PICK1 to the ubiquitously expressed PACSIN2 is also regulated by the homologous phosphorylation sites within the PACSIN2-variable region. Genetic deletion of PACSIN2, which is highly expressed in Purkinje cells, eliminates cerebellar long-term depression. This deficit can be fully rescued by overexpressing wild-type PACSIN2, but not by a PACSIN2 phosphomimetic mutant, which does not bind PICK1 efficiently. Taken together, our data demonstrate that the interaction of PICK1 and PACSIN is required for the activity-dependent internalization of AMPARs and for the expression of long-term depression in the cerebellum.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.