ArticleProceedings of the National Academy of Sciences of the United States of America2016
How curvature-generating proteins build scaffolds on membrane nanotubes.
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 85 papers.
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Who cites it
85 citing papers in PubMed, 146 citations in OpenAlex.
- Subdomains of endophilin can drive membrane remodeling and facilitate controlled membrane scission.Biophysical journal · 2026Article
- Intra-cluster receptor density (IRD): A molecular switch for TNFR1 clusters' signaling.Science advances · 2026Article
- Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026Review
- From molecular mechanisms of glycosphingolipid function to bio-therapeutic applications.Cellular and molecular life sciences : CMLS · 2026Review
- Article
- Subdomains of Endophilin-NBAR Can Synergistically Drive Membrane Remodeling and Facilitate Controlled Membrane Scission.bioRxiv : the preprint server for biology · 2026Article
- Friction-driven scission: How nonlocal mechanisms contribute to membrane fission across domains of life.Science advances · 2026Review
- Bending the boundaries: the many facets of endophilin-As from membrane dynamics to disease.Cellular and molecular life sciences : CMLS · 2025Review
- GTP hydrolysis triggers membrane remodeling by AMPH-1.Science advances · 2025Article
- Long-Range Interactions Between Neighboring Nanoparticles Tuned by Confining Membranes.Nanomaterials (Basel, Switzerland) · 2025Article
- Coordination of force-generating actin-based modules stabilizes and remodels membranes in vivo.The Journal of cell biology · 2024Article
- Assembly and fission of tubular carriers mediating protein sorting in endosomes.Nature reviews. Molecular cell biology · 2024Review
- Research progress on the regulatory role of cell membrane surface tension in cell behavior.Heliyon · 2024Review
- Molecular basis for curvature formation in SepF polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Amphipathic Helices Can Sense Both Positive and Negative Curvatures of Lipid Membranes.The journal of physical chemistry letters · 2024Article
- Membrane shapers from two distinct superfamilies cooperate in the development of neuronal morphology.The Journal of cell biology · 2023Article
- Membrane free-energy landscapes derived from atomistic dynamics explain nonuniversal cholesterol-induced stiffening.PNAS nexus · 2023Article
- Dynamics of upstream ESCRT organization at the HIV-1 budding site.Biophysical journal · 2023Article
- Morphogenesis of starfish polymersomes.Nature communications · 2023Article
- Out of the ESCPE room: Emerging roles of endosomal SNX-BARs in receptor transport and host-pathogen interaction.Traffic (Copenhagen, Denmark) · 2023Review
25 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
Bin/Amphiphysin/Rvs (BAR) domain proteins control the curvature of lipid membranes in endocytosis, trafficking, cell motility, the formation of complex subcellular structures, and many other cellular phenomena. They form 3D assemblies that act as molecular scaffolds to reshape the membrane and alter its mechanical properties. It is unknown, however, how a protein scaffold forms and how BAR domains interact in these assemblies at protein densities relevant for a cell. In this work, we use various experimental, theoretical, and simulation approaches to explore how BAR proteins organize to form a scaffold on a membrane nanotube. By combining quantitative microscopy with analytical modeling, we demonstrate that a highly curving BAR protein endophilin nucleates its scaffolds at the ends of a membrane tube, contrary to a weaker curving protein centaurin, which binds evenly along the tube's length. Our work implies that the nature of local protein-membrane interactions can affect the specific localization of proteins on membrane-remodeling sites. Furthermore, we show that amphipathic helices are dispensable in forming protein scaffolds. Finally, we explore a possible molecular structure of a BAR-domain scaffold using coarse-grained molecular dynamics simulations. Together with fluorescence microscopy, the simulations show that proteins need only to cover 30-40% of a tube's surface to form a rigid assembly. Our work provides mechanical and structural insights into the way BAR proteins may sculpt the membrane as a high-order cooperative assembly in important biological processes.
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Registered trials
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.