Evidence map›Paper›PMID 31816055›Full record

ArticleThe Journal of cell biology2020

Relief of talin autoinhibition triggers a force-independent association with vinculin.

Paul Atherton, Franziska Lausecker, Alexandre Carisey, Andrew Gilmore, David Critchley, Igor Barsukov, Christoph Ballestrem

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Integrins in the kidney - beyond the matrix.Nature reviews. Nephrology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Allosteric activation of vinculin by talin.Nature communications · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Review
  15. Article
  16. Talin‑1 interaction network in cellular mechanotransduction (Review).International journal of molecular medicine · 2022
    Review
  17. Viscoelasticity, Like Forces, Plays a Role in Mechanotransduction.Frontiers in cell and developmental biology · 2022
    Review
  18. Review
  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

7 authors at 3 institutions in 1 country.

Paul AthertonWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Franziska LauseckerWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Alexandre CariseyWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Andrew GilmoreWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
David CritchleyDepartment of Biochemistry, University of Leicester, Leicester, UK.
Igor BarsukovInstitute of Integrative Biology, University of Liverpool, Liverpool, UK.
Christoph BallestremWellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.
Wellcome Centre for Cell-Matrix Research · GBUniversity of Leicester · GBUniversity of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M01150X/1Biotechnology and Biological Sciences Research Council BB/P000681/1Wellcome TrustWellcome Trust 202860/Z/16/ZWellcome Trust 203128/Z/16/Z
6 · The paper itself

Abstract

Talin, vinculin, and paxillin are core components of the dynamic link between integrins and actomyosin. Here, we study the mechanisms that mediate their activation and association using a mitochondrial-targeting assay, structure-based mutants, and advanced microscopy. As expected, full-length vinculin and talin are autoinhibited and do not interact with each other. However, contrary to previous models that propose a critical role for forces driving talin-vinculin association, our data show that force-independent relief of autoinhibition is sufficient to mediate their tight interaction. We also found that paxillin can bind to both talin and vinculin when either is inactive. Further experiments demonstrated that adhesions containing paxillin and vinculin can form without talin following integrin activation. However, these are largely deficient in exerting traction forces to the matrix. Our observations lead to a model whereby paxillin contributes to talin and vinculin recruitment into nascent adhesions. Activation of the talin-vinculin axis subsequently leads to the engagement with the traction force machinery and focal adhesion maturation.

Indexed as

Stress, MechanicalActin CytoskeletonAnimalsCells, CulturedFibroblastsFocal AdhesionsMiceMice, Inbred C57BLMice, KnockoutPaxillinProtein BindingTalinVinculinPaxillinPxn protein, mouseTalinTln1 protein, mouseVcl protein, mouseVinculin

Identifiers

PMID31816055
PMCPMC7039207
OpenAlexW2991919384

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.