ArticleStructure (London, England : 1993)2015
Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- Utilizing AfDesign for Developing a Small Molecule Inhibitor of PICK- 1-PDZ.Current protein & peptide science · 2025Article
- Unconventional PDZ Recognition Revealed in α7 nAChR-PICK1 Complexes.ACS chemical neuroscience · 2024Article
- Small-Angle X-Ray Scattering for Macromolecular Complexes.Advances in experimental medicine and biology · 2024Article
- Investigating the allosteric response of the PICK1 PDZ domain to different ligands with all-atom simulations.Protein science : a publication of the Protein Society · 2022Article
- Article
- Review
- Coding variants identified in patients with diabetes alter PICK1 BAR domain function in insulin granule biogenesis.The Journal of clinical investigation · 2022Article
- CaFrontiers in molecular neuroscience · 2022Article
- The intracellular lipid-binding domain of human NaCommunications biology · 2020Article
- 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
- Residue-Level Contact Reveals Modular Domain Interactions of PICK1 Are Driven by Both Electrostatic and Hydrophobic Forces.Frontiers in molecular biosciences · 2020Article
- PDZ Domains as Drug Targets.Advanced therapeutics · 2019Review
- ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.PLoS computational biology · 2019Article
- AMPA receptors and their minions: auxiliary proteins in AMPA receptor trafficking.Cellular and molecular life sciences : CMLS · 2019Review
- Mechanisms of PDZ domain scaffold assembly illuminated by use of supported cell membrane sheets.eLife · 2019Article
- Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019Review
- Arc/Arg3.1 has an activity-regulated interaction with PICK1 that results in altered spatial dynamics.Scientific reports · 2018Article
- The Regulation of AMPA Receptor Endocytosis by Dynamic Protein-Protein Interactions.Frontiers in cellular neuroscience · 2018Article
- Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017Review
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Authors and funding
17 authors at 3 institutions in 2 countries.
Funding
Abstract
PICK1 is a neuronal scaffolding protein containing a PDZ domain and an auto-inhibited BAR domain. BAR domains are membrane-sculpting protein modules generating membrane curvature and promoting membrane fission. Previous data suggest that BAR domains are organized in lattice-like arrangements when stabilizing membranes but little is known about structural organization of BAR domains in solution. Through a small-angle X-ray scattering (SAXS) analysis, we determine the structure of dimeric and tetrameric complexes of PICK1 in solution. SAXS and biochemical data reveal a strong propensity of PICK1 to form higher-order structures, and SAXS analysis suggests an offset, parallel mode of BAR-BAR oligomerization. Furthermore, unlike accessory domains in other BAR domain proteins, the positioning of the PDZ domains is flexible, enabling PICK1 to perform long-range, dynamic scaffolding of membrane-associated proteins. Together with functional data, these structural findings are compatible with a model in which oligomerization governs auto-inhibition of BAR domain function.
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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.