Evidence map›Paper›PMID 28818948›Full record

ArticleScience (New York, N.Y.)2017

Vinculin forms a directionally asymmetric catch bond with F-actin.

Derek L Huang, Nicolas A Bax, Craig D Buckley, William I Weis, Alexander R Dunn

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 168 papers.

0numbers the graph read from it
0cells of the map it votes in
168citing papers in PubMed
14.0field-weighted citation impact, top 1% of its field
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

168 citing papers in PubMed, 298 citations in OpenAlex.

  1. Article
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  6. Review
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  9. Modulation of the Mechanosensory Matrisome by Serotonergic Signaling.Results and problems in cell differentiation · 2026
    Review
  10. Article
  11. Review
  12. Article
  13. The mechanical response of vinculin.Science advances · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. A direct computational assessment of vinculin-actin unbinding kinetics reveals catch-bonding behavior.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Derek L HuangBiophysics Program, Stanford University, Stanford, CA 94305, USA.ORCID 0000-0003-1502-928X
Nicolas A BaxDepartment of Structural Biology, Stanford University, Stanford, CA 94305, USA.ORCID 0000-0003-2535-7666
Craig D BuckleyDepartment of Chemical Engineering, Stanford University, Stanford, CA 94305, USA.
William I WeisBiophysics Program, Stanford University, Stanford, CA 94305, USA. bill.weis@stanford.edu alex.dunn@stanford.edu.ORCID 0000-0002-5583-6150
Alexander R DunnBiophysics Program, Stanford University, Stanford, CA 94305, USA. bill.weis@stanford.edu alex.dunn@stanford.edu.ORCID 0000-0001-6096-4600
Stanford University · USCardiovascular Institute of the South · US

Funding

Supplement to Enhance Wellness and Resiliency in the Graduate EnvironmentT32GM007276 · NIGMS · STANFORD UNIVERSITY · PI MORRISON, ASHBY J. · 1985 to 2023
$32.9M
Molecular Biophysics Training Program at StanfordT32GM008294 · NIGMS · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 1989 to 2019
$7.4M
Molecular mechanisms underlying force sensing at intercellular junctionsR01GM117457 · NIGMS · STANFORD UNIVERSITY · PI DUNN, ALEXANDER R, WEIS, WILLIAM I · 2016 to 2019
$1.5M
The function of MEKK3 interaction with CCM2R01GM114621 · NIGMS · YALE UNIVERSITY · PI BOGGON, TITUS JONATHON, SU, BING · 2015 to 2018
$1.3M
Understanding force-dependent binding of alpha-catenin to actinR01GM114462 · NIGMS · STANFORD UNIVERSITY · PI DUNN, ALEXANDER R, WEIS, WILLIAM I · 2015 to 2018
$1.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM114462NIGMS NIH HHS R01 GM114621NIGMS NIH HHS R01 GM117457NIGMS NIH HHS T32 GM007276NIGMS NIH HHS T32 GM008294
6 · The paper itself

Abstract

Vinculin is an actin-binding protein thought to reinforce cell-cell and cell-matrix adhesions. However, how mechanical load affects the vinculin-F-actin bond is unclear. Using a single-molecule optical trap assay, we found that vinculin forms a force-dependent catch bond with F-actin through its tail domain, but with lifetimes that depend strongly on the direction of the applied force. Force toward the pointed (-) end of the actin filament resulted in a bond that was maximally stable at 8 piconewtons, with a mean lifetime (12 seconds) 10 times as long as the mean lifetime when force was applied toward the barbed (+) end. A computational model of lamellipodial actin dynamics suggests that the directionality of the vinculin-F-actin bond could establish long-range order in the actin cytoskeleton. The directional and force-stabilized binding of vinculin to F-actin may be a mechanism by which adhesion complexes maintain front-rear asymmetry in migrating cells.

Indexed as

Models, ChemicalActin CytoskeletonActinsCell MovementComputer SimulationOptical TweezersProtein BindingPseudopodiaSingle Molecule ImagingVinculinActinsVinculin

Identifiers

PMID28818948
PMCPMC5821505
OpenAlexW2749092846

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.