ArticleNature cell biology2012
Membrane bending by protein-protein crowding.
Article in Nature cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 279 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
279 citing papers in PubMed.
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- Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026Review
- Mapping Protein Diffusion from the Plasma Membrane to the Nucleus: Insights from Fluorescence Correlation Spectroscopy.Biomolecules · 2026Review
- A co-overexpression strategy allows effective protein-protein binding affinities to be assessed as a function of concentration within live cells.bioRxiv : the preprint server for biology · 2026Article
- Shaping Function: Polymeric 3D Systems With Unconventional Geometries for Biomedical Applications.Small (Weinheim an der Bergstrasse, Germany) · 2026Review
- Ion- and Temperature-Programmable Reconfiguration of Subcompartments in Synthetic Cells.Chembiochem : a European journal of chemical biology · 2026Article
- Physiological implications of phase separation in vesicle organization and trafficking.BMC biology · 2026Review
- Cannabidiol (CBD) Induces Lipid Microdomain Disruption or Budding in Ternary Mixtures.The journal of physical chemistry. B · 2026Article
- VAMP8 function reveals tight linkage between endocytic recycling and endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Clathrin is an Intrinsic Driver of Membrane Fission.bioRxiv : the preprint server for biology · 2026Article
- Linear ubiquitination triggers Amph-mediated T-tubule biogenesis.Science advances · 2026Article
- Topography-driven movement of biomolecular condensates.PloS one · 2026Article
- Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025Review
- Cholesterol modulates membrane elasticity via unified biophysical laws.Nature communications · 2025Article
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Article
- Cellular Signaling at the Nano-Bio Interface: Spotlighting Membrane Curvature.Annual review of physical chemistry · 2025Review
219 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Curved membranes are an essential feature of dynamic cellular structures, including endocytic pits, filopodia protrusions and most organelles. It has been proposed that specialized proteins induce curvature by binding to membranes through two primary mechanisms: membrane scaffolding by curved proteins or complexes; and insertion of wedge-like amphipathic helices into the membrane. Recent computational studies have raised questions about the efficiency of the helix-insertion mechanism, predicting that proteins must cover nearly 100% of the membrane surface to generate high curvature, an improbable physiological situation. Thus, at present, we lack a sufficient physical explanation of how protein attachment bends membranes efficiently. On the basis of studies of epsin1 and AP180, proteins involved in clathrin-mediated endocytosis, we propose a third general mechanism for bending fluid cellular membranes: protein-protein crowding. By correlating membrane tubulation with measurements of protein densities on membrane surfaces, we demonstrate that lateral pressure generated by collisions between bound proteins drives bending. Whether proteins attach by inserting a helix or by binding lipid heads with an engineered tag, protein coverage above ~20% is sufficient to bend membranes. Consistent with this crowding mechanism, we find that even proteins unrelated to membrane curvature, such as green fluorescent protein (GFP), can bend membranes when sufficiently concentrated. These findings demonstrate a highly efficient mechanism by which the crowded protein environment on the surface of cellular membranes can contribute to membrane shape change.
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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.