Evidence map›Paper›PMID 35245171›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

The C-terminal actin-binding domain of talin forms an asymmetric catch bond with F-actin.

Leanna M Owen, Nicolas A Bax, William I Weis, Alexander R Dunn

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
7.9field-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

46 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. 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
  7. Environmental Toxicants and Their Disruption of Integrin Signaling in Lipid Rafts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  8. Review
  9. Biochemical and structural bases for talin ABSs-F-actin interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. De novo DNA-based catch bonds.Nature chemistry · 2024
    Article
  15. Article
  16. Principles and regulation of mechanosensing.Journal of cell science · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Leanna M OwenBiophysics Program, Stanford University, Stanford, CA 94305.ORCID 0000-0001-7339-7895
Nicolas A BaxChemical Engineering, Stanford University, Stanford, CA 94305.ORCID 0000-0003-2535-7666
William I WeisBiophysics Program, Stanford University, Stanford, CA 94305.ORCID 0000-0002-5583-6150
Alexander R DunnBiophysics Program, Stanford University, Stanford, CA 94305.ORCID 0000-0001-6096-4600
Stanford University · US

Funding

Supplement to Enhance Wellness and Resiliency in the Graduate EnvironmentT32GM007276 · NIGMS · STANFORD UNIVERSITY · PI MORRISON, ASHBY J. · 1985 to 2023
$32.9M
INSTITUTIONAL TRAINING GRANT IN GENOME SCIENCET32HG000044 · NHGRI · STANFORD UNIVERSITY · PI MICHAEL P. SNYDER · 1995 to 2026
$32.2M
Molecular Biophysics Training Program at StanfordT32GM008294 · NIGMS · STANFORD UNIVERSITY · PI HUANG, KERWYN C. · 1989 to 2019
$7.4M
Molecular mechanisms underlying force transduction at cellular adhesion complexesR35GM130332 · NIGMS · STANFORD UNIVERSITY · PI Alexander R Dunn · 2019 to 2026
$4.9M
Molecular mechanisms of Wnt and mechanical signaling through β-cateninR35GM131747 · NIGMS · STANFORD UNIVERSITY · PI POKUTTA, SABINE · 2019 to 2023
$3.1M
Understanding force-dependent binding of alpha-catenin to actinR01GM114462 · NIGMS · STANFORD UNIVERSITY · PI DUNN, ALEXANDER R, WEIS, WILLIAM I · 2015 to 2018
$1.2M
NHGRI NIH HHS T32 HG000044NIGMS NIH HHS R01 GM114462NIGMS NIH HHS R35 GM130332NIGMS NIH HHS R35 GM131747NIGMS NIH HHS T32 GM007276NIGMS NIH HHS T32 GM008294
6 · The paper itself

Abstract

SignificanceTalin is a mechanosensitive adaptor protein that links integrins to the actin cytoskeleton at cell-extracellular matrix adhesions. Although the C-terminal actin-binding domain ABS3 of talin is required for function, it binds weakly to actin in solution. We show that ABS3 binds actin strongly only when subjected to mechanical forces comparable to those generated by the cytoskeleton. Moreover, the interaction between ABS3 and actin depends strongly on the direction of force in a manner predicted to organize actin to facilitate adhesion growth and efficient cytoskeletal force generation. These characteristics can explain how force sensing by talin helps to nucleate adhesions precisely when and where they are required to transmit force between the cytoskeleton and the extracellular matrix.

Indexed as

ActinsAnimalsHumansProtein BindingProtein DomainsTalinActinsTalinTLN1 protein, humancatch bondF-actinfocal adhesiontalin

Identifiers

PMID35245171
PMCPMC8915792
OpenAlexW4220814163

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.