Evidence map›Paper›PMID 32657269›Full record

ArticleeLife2020

Phosphoinositides regulate force-independent interactions between talin, vinculin, and actin.

Charlotte F Kelley, Thomas Litschel, Stephanie Schumacher, Dirk Dedden, Petra Schwille, Naoko Mizuno

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  6. Environmental Toxicants and Their Disruption of Integrin Signaling in Lipid Rafts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  7. Article
  8. 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
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
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  15. Article
  16. Allosteric activation of vinculin by talin.Nature communications · 2023
    Article
  17. Article
  18. Review
  19. Review
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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

6 authors at 2 institutions in 2 countries.

Charlotte F KelleyMax Planck Institute of Biochemistry, Department of Structural Cell Biology, Martinsried, Germany.ORCID 0000-0002-7684-9049
Thomas LitschelMax Planck Institute of Biochemistry, Department of Cellular and Molecular Biophysics, Martinsried, Germany.ORCID 0000-0001-7123-8364
Stephanie SchumacherMax Planck Institute of Biochemistry, Department of Structural Cell Biology, Martinsried, Germany.
Dirk DeddenMax Planck Institute of Biochemistry, Department of Structural Cell Biology, Martinsried, Germany.ORCID 0000-0003-3630-1270
Petra SchwilleMax Planck Institute of Biochemistry, Department of Cellular and Molecular Biophysics, Martinsried, Germany.ORCID 0000-0002-6106-4847
Naoko MizunoMax Planck Institute of Biochemistry, Department of Structural Cell Biology, Martinsried, Germany.ORCID 0000-0002-1594-2821
Max Planck Institute of Biochemistry · DENational Institutes of Health · US

Funding

Alexander von Humboldt-Stiftung Research Fellowship for Postdoctoral ResearchersBoehringer Ingelheim Stiftung Plus 3European Molecular Biology Organization EMBO Long-term Fellowship AwardEuropean Molecular Biology Organization Young Investigator AwardH2020 European Research Council FocAdHorizon 2020 Framework Programme Marie Sklodowska-Curie Action
6 · The paper itself

Abstract

Focal adhesions (FA) are large macromolecular assemblies which help transmit mechanical forces and regulatory signals between the extracellular matrix and an interacting cell. Two key proteins talin and vinculin connecting integrin to actomyosin networks in the cell. Both proteins bind to F-actin and each other, providing a foundation for network formation within FAs. However, the underlying mechanisms regulating their engagement remain unclear. Here, we report on the results of in vitro reconstitution of talin-vinculin-actin assemblies using synthetic membrane systems. We find that neither talin nor vinculin alone recruit actin filaments to the membrane. In contrast, phosphoinositide-rich membranes recruit and activate talin, and the membrane-bound talin then activates vinculin. Together, the two proteins then link actin to the membrane. Encapsulation of these components within vesicles reorganized actin into higher-order networks. Notably, these observations were made in the absence of applied force, whereby we infer that the initial assembly stage of FAs is force independent. Our findings demonstrate that the local membrane composition plays a key role in controlling the stepwise recruitment, activation, and engagement of proteins within FAs.

Indexed as

Actin CytoskeletonActinsMembranes, ArtificialPhosphatidylinositolsTalinVinculinActinsMembranes, ArtificialPhosphatidylinositolsTalinTLN2 protein, humanVCL protein, humanVinculinactinautoinhibitioncell biologyfocal adhesionmolecular biophysicsnonePI(4,5)P2structural biologytalinvinculin

Identifiers

PMID32657269
PMCPMC7384861
OpenAlexW3041675330

What OpenQuestion holds

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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.