ArticleMolecular biology of the cell2015
PICK1 is implicated in organelle motility in an Arp2/3 complex-independent manner.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Cytochalasin B Mitigates the Inflammatory Response in Lipopolysaccharide-Induced Mastitis by Suppressing Both the ARPC3/ARPC4-Dependent Cytoskeletal Changes and the Association Between HSP70 and the NLRP3 Inflammasome.International journal of molecular sciences · 2025Article
- The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025Review
- Unconventional PDZ Recognition Revealed in α7 nAChR-PICK1 Complexes.ACS chemical neuroscience · 2024Article
- Nucleation, stabilization, and disassembly of branched actin networks.Trends in cell biology · 2022Review
- Molecular mechanism of Arp2/3 complex inhibition by Arpin.Nature communications · 2022Article
- The BAR domain of the Arf GTPase-activating protein ASAP1 directly binds actin filaments.The Journal of biological chemistry · 2020Article
- A high-affinity, bivalent PDZ domain inhibitor complexes PICK1 to alleviate neuropathic pain.EMBO molecular medicine · 2020Article
- Cryo-EM structure of NPF-bound human Arp2/3 complex and activation mechanism.Science advances · 2020Article
- Residue-Level Contact Reveals Modular Domain Interactions of PICK1 Are Driven by Both Electrostatic and Hydrophobic Forces.Frontiers in molecular biosciences · 2020Article
- Palmitoylated Proteins in Dendritic Spine Remodeling.Frontiers in synaptic neuroscience · 2020Article
- Cellular and pathophysiological consequences of Arp2/3 complex inhibition: role of inhibitory proteins and pharmacological compounds.Cellular and molecular life sciences : CMLS · 2019Review
- PDZ Domains as Drug Targets.Advanced therapeutics · 2019Review
- AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking.Cellular and molecular life sciences : CMLS · 2019Review
- 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
- Fam49/CYRI interacts with Rac1 and locally suppresses protrusions.Nature cell biology · 2018Article
- Cortactin regulates endo-lysosomal sorting of AMPARs via direct interaction with GluA2 subunit.Scientific reports · 2018Article
- The Regulation of AMPA Receptor Endocytosis by Dynamic Protein-Protein Interactions.Frontiers in cellular neuroscience · 2018Article
- PICK1 regulates AMPA receptor endocytosis via direct interactions with AP2 α-appendage and dynamin.The Journal of cell biology · 2017Article
- Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017Review
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8 authors at 1 institution in 1 country.
Funding
Abstract
PICK1 is a modular scaffold implicated in synaptic receptor trafficking. It features a PDZ domain, a BAR domain, and an acidic C-terminal tail (ACT). Analysis by small- angle x-ray scattering suggests a structural model that places the receptor-binding site of the PDZ domain and membrane-binding surfaces of the BAR and PDZ domains adjacent to each other on the concave side of the banana-shaped PICK1 dimer. In the model, the ACT of one subunit of the dimer interacts with the PDZ and BAR domains of the other subunit, possibly accounting for autoinhibition. Consistently, full-length PICK1 shows diffuse cytoplasmic localization, but it clusters on vesicle-like structures that colocalize with the trans-Golgi network marker TGN38 upon deletion of either the ACT or PDZ domain. This localization is driven by the BAR domain. Live-cell imaging further reveals that PICK1-associated vesicles undergo fast, nondirectional motility in an F-actin-dependent manner, but deleting the ACT dramatically reduces vesicle speed. Thus the ACT links PICK1-associated vesicles to a motility factor, likely myosin, but, contrary to previous reports, PICK1 neither binds nor inhibits Arp2/3 complex.
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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.