Evidence map›Paper›PMID 23974298›Full record

ArticleCellular and molecular life sciences : CMLS2014

CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics.

Radoslav Janoštiak, Jan Brábek, Vera Auernheimer, Zuzana Tatárová, Lena A Lautscham, Tuli Dey, Jakub Gemperle, Rudolf Merkel, Wolfgang H Goldmann, Ben Fabry and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 61 citations in OpenAlex.

  1. The mechanical response of vinculin.Science advances · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  8. p130Cas/Frontiers in cell and developmental biology · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Vinculin in cell-cell and cell-matrix adhesions.Cellular and molecular life sciences : CMLS · 2017
    Review
  16. Molecular stretching modulates mechanosensing pathways.Protein science : a publication of the Protein Society · 2017
    Review
  17. Article
  18. Article
  19. Review
  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

11 authors at 3 institutions in 2 countries.

Radoslav JanoštiakDepartment of Cell Biology, Faculty of Science, Charles University in Prague, Czech Republic, Vinicna 7, 128 43, Prague, Czech Republic.
Jan Brábek
Vera Auernheimer
Zuzana Tatárová
Lena A Lautscham
Tuli Dey
Jakub Gemperle
Rudolf Merkel
Wolfgang H Goldmann
Ben Fabry
Daniel Rösel
Charles University · CZFriedrich-Alexander-Universität Erlangen-Nürnberg · DEForschungszentrum Jülich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Focal adhesions are cellular structures through which both mechanical forces and regulatory signals are transmitted. Two focal adhesion-associated proteins, Crk-associated substrate (CAS) and vinculin, were both independently shown to be crucial for the ability of cells to transmit mechanical forces and to regulate cytoskeletal tension. Here, we identify a novel, direct binding interaction between CAS and vinculin. This interaction is mediated by the CAS SRC homology 3 domain and a proline-rich sequence in the hinge region of vinculin. We show that CAS localization in focal adhesions is partially dependent on vinculin, and that CAS-vinculin coupling is required for stretch-induced activation of CAS at the Y410 phosphorylation site. Moreover, CAS-vinculin binding significantly affects the dynamics of CAS and vinculin within focal adhesions as well as the size of focal adhesions. Finally, disruption of CAS binding to vinculin reduces cell stiffness and traction force generation. Taken together, these findings strongly implicate a crucial role of CAS-vinculin interaction in mechanosensing and focal adhesion dynamics.

Indexed as

Amino Acid MotifsAnimalsBiomechanical PhenomenaCell AdhesionCell LineCrk-Associated Substrate ProteinFibroblastsFocal Adhesion Protein-Tyrosine KinasesFocal AdhesionsMicePeptidesPhosphorylationProtein BindingProtein Interaction Mapssrc Homology DomainsVinculinCrk-Associated Substrate ProteinFocal Adhesion Protein-Tyrosine KinasesPeptidespolyprolineVinculin

Identifiers

PMID23974298
PMCPMC3901934
OpenAlexW2121749477

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.