ArticleMolecular biology of the cell2013
Formation of membrane ridges and scallops by the F-BAR protein Nervous Wreck.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- ASFV pE146L-induced ER remodeling is essential for viral replication.Journal of virology · 2025Article
- From function to structure: how myofibrillogenesis influences the transverse-axial tubular system development and its peculiarities.Frontiers in physiology · 2025Review
- Endosomal actin branching, fission, and receptor recycling require FCHSD2 recruitment by MICAL-L1.Molecular biology of the cell · 2024Article
- Membrane-induced 2D phase separation of the focal adhesion protein talin.Nature communications · 2024Article
- Filopodial protrusion driven by density-dependent Ena-TOCA-1 interactions.Journal of cell science · 2024Article
- An approach for quantitative mapping of synaptic periactive zone architecture and organization.Molecular biology of the cell · 2023Article
- Plasma membrane topography governs the 3D dynamic localization of IgM B cell antigen receptor clusters.The EMBO journal · 2023Article
- The state of F-BAR domains as membrane-bound oligomeric platforms.Trends in cell biology · 2021Review
- Article
- Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin.eLife · 2020Article
- Higher-order assembly of Sorting Nexin 16 controls tubulation and distribution of neuronal endosomes.The Journal of cell biology · 2019Article
- Opposing functions of F-BAR proteins in neuronal membrane protrusion, tubule formation, and neurite outgrowth.Life science alliance · 2019Article
- Role for ERK1/2-dependent activation of FCHSD2 in cancer cell-selective regulation of clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Coordinated autoinhibition of F-BAR domain membrane binding and WASp activation by Nervous Wreck.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Linking up at the BAR: Oligomerization and F-BAR protein function.Cell cycle (Georgetown, Tex.) · 2016Review
- The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis.Cell reports · 2016Article
- BAR-SH3 sorting nexins are conserved interacting proteins of Nervous wreck that organize synapses and promote neurotransmission.Journal of cell science · 2016Article
- Membrane Charge Directs the Outcome of F-BAR Domain Lipid Binding and Autoregulation.Cell reports · 2015Article
- Oligomerization but Not Membrane Bending Underlies the Function of Certain F-BAR Proteins in Cell Motility and Cytokinesis.Developmental cell · 2015Article
- Depletion or over-expression of Sh3px1 results in dramatic changes in cell morphology.Biology open · 2015Article
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9 authors.
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Abstract
Eukaryotic cells are defined by extensive intracellular compartmentalization, which requires dynamic membrane remodeling. FER/Cip4 homology-Bin/amphiphysin/Rvs (F-BAR) domain family proteins form crescent-shaped dimers, which can bend membranes into buds and tubules of defined geometry and lipid composition. However, these proteins exhibit an unexplained wide diversity of membrane-deforming activities in vitro and functions in vivo. We find that the F-BAR domain of the neuronal protein Nervous Wreck (Nwk) has a novel higher-order structure and membrane-deforming activity that distinguishes it from previously described F-BAR proteins. The Nwk F-BAR domain assembles into zigzags, creating ridges and periodic scallops on membranes in vitro. This activity depends on structural determinants at the tips of the F-BAR dimer and on electrostatic interactions of the membrane with the F-BAR concave surface. In cells, Nwk-induced scallops can be extended by cytoskeletal forces to produce protrusions at the plasma membrane. Our results define a new F-BAR membrane-deforming activity and illustrate a molecular mechanism by which positively curved F-BAR domains can produce a variety of membrane curvatures. These findings expand the repertoire of F-BAR domain mediated membrane deformation and suggest that unique modes of higher-order assembly can define how these proteins sculpt the membrane.
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