ArticleProceedings of the National Academy of Sciences of the United States of America2016
Coordinated autoinhibition of F-BAR domain membrane binding and WASp activation by Nervous Wreck.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Article
- Chemical and Mechanical Regulation of Leukocyte Migration.Cold Spring Harbor perspectives in biology · 2026Review
- Deployment of endocytic machinery to periactive zones of nerve terminals is independent of active zone assembly and evoked release.bioRxiv : the preprint server for biology · 2026Article
- Ubiquitylation-dependent Rap2 activation regulates lamellipodia dynamics during cell migration.Journal of cell science · 2025Article
- Computer Simulations Show That Liquid-Liquid Phase Separation Enhances Self-Assembly.ACS nano · 2025Article
- F-BAR Proteins CIP4 and FBP17 Function in Cortical Neuron Radial Migration and Process Outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Characterization of atypical BAR domain-containing proteins coded by Toxoplasma gondii.The Journal of biological chemistry · 2024Article
- Endosomal actin branching, fission, and receptor recycling require FCHSD2 recruitment by MICAL-L1.Molecular biology of the cell · 2024Article
- Sensing their plasma membrane curvature allows migrating cells to circumvent obstacles.Nature communications · 2023Article
- An approach for quantitative mapping of synaptic periactive zone architecture and organization.Molecular biology of the cell · 2023Article
- Self-assembly coupled to liquid-liquid phase separation.PLoS computational biology · 2023Article
- Spatio-temporal regulation of endocytic protein assembly by SH3 domains in yeast.Molecular biology of the cell · 2023Article
- Fission yeast paxillin contains two Cdc15 binding motifs for robust recruitment to the cytokinetic ring.Molecular biology of the cell · 2022Article
- Dendritic Spine Initiation in Brain Development, Learning and Diseases and Impact of BAR-Domain Proteins.Cells · 2021Review
- The state of F-BAR domains as membrane-bound oligomeric platforms.Trends in cell biology · 2021Review
- Article
- Pay attention to membrane tension: Mechanobiology of the cell surface.Current opinion in cell biology · 2020Review
- The cryo-EM structure of the SNX-BAR Mvp1 tetramer.Nature communications · 2020Article
- Opposing functions of F-BAR proteins in neuronal membrane protrusion, tubule formation, and neurite outgrowth.Life science alliance · 2019Article
- BAR domain proteins-a linkage between cellular membranes, signaling pathways, and the actin cytoskeleton.Biophysical reviews · 2018Review
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7 authors.
Funding
Abstract
Membrane remodeling by Fes/Cip4 homology-Bin/Amphiphysin/Rvs167 (F-BAR) proteins is regulated by autoinhibitory interactions between their SRC homology 3 (SH3) and F-BAR domains. The structural basis of autoregulation, and whether it affects interactions of SH3 domains with other cellular ligands, remain unclear. Here we used single-particle electron microscopy to determine the structure of the F-BAR protein Nervous Wreck (Nwk) in both soluble and membrane-bound states. On membrane binding, Nwk SH3 domains do not completely dissociate from the F-BAR dimer, but instead shift from its concave surface to positions on either side of the dimer. Unexpectedly, along with controlling membrane binding, these autoregulatory interactions inhibit the ability of Nwk-SH3a to activate Wiskott-Aldrich syndrome protein (WASp)/actin related protein (Arp) 2/3-dependent actin filament assembly. In Drosophila neurons, Nwk autoregulation restricts SH3a domain-dependent synaptopod formation, synaptic growth, and actin organization. Our results define structural rearrangements in Nwk that control F-BAR-membrane interactions as well as SH3 domain activities, and suggest that these two functions are tightly coordinated in vitro and in vivo.
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