Evidence map›Paper›PMID 22902598›Full record

ArticleNature cell biology2012

Membrane bending by protein-protein crowding.

Jeanne C Stachowiak, Eva M Schmid, Christopher J Ryan, Hyoung Sook Ann, Darryl Y Sasaki, Michael B Sherman, Phillip L Geissler, Daniel A Fletcher, Carl C Hayden

Abstract read
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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.

0numbers the graph read from it
0cells of the map it votes in
279citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

279 citing papers in PubMed.

  1. Visualization of membrane-stabilized SorCS2Journal of structural biology: X · 2026
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  5. Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026
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  9. Ion- and Temperature-Programmable Reconfiguration of Subcompartments in Synthetic Cells.Chembiochem : a European journal of chemical biology · 2026
    Article
  10. Review
  11. Article
  12. VAMP8 function reveals tight linkage between endocytic recycling and endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Clathrin is an Intrinsic Driver of Membrane Fission.bioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Article
  16. Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025
    Review
  17. Article
  18. Review
  19. Article
  20. Review

219 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Jeanne C StachowiakThe University of Texas at Austin, Department of Biomedical Engineering, Austin, Texas 78712, USA. jcstach@austin.utexas.edu
Eva M Schmid
Christopher J Ryan
Hyoung Sook Ann
Darryl Y Sasaki
Michael B Sherman
Phillip L Geissler
Daniel A Fletcher
Carl C Hayden

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Adaptor Proteins, Vesicular TransportAmino Acid SequenceCell MembraneMembrane ProteinsMolecular Sequence DataMonomeric Clathrin Assembly ProteinsProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryAdaptor Proteins, Vesicular Transportclathrin assembly protein AP180epsinMembrane ProteinsMonomeric Clathrin Assembly Proteins

Identifiers

PMID22902598

What OpenQuestion holds

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Registered trials

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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.