Evidence map›Paper›PMID 38087085›Full record

ArticleNature structural & molecular biology2023

Talin and kindlin use integrin tail allostery and direct binding to activate integrins.

Jonas Aretz, Masood Aziz, Nico Strohmeyer, Michael Sattler, Reinhard Fässler

Open access · hybridAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
9.2field-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

30 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
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  6. Review
  7. Synergistic effect of PIPBiophysical journal · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Functional unfolding of the integrin αX transmembrane helix.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Compressed Cells Facilitate Adhesion Through Glycocalyx.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  15. Kindlin Regulates Mechanosensitive Activation and Adhesion Assembly of Integrin beta6.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  16. Article
  17. Article
  18. Article
  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

5 authors at 3 institutions in 2 countries.

Jonas AretzDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-4623-5820
Masood AzizDepartment of Bioscience, Technical University of Munich, TUM School of Natural Sciences, Garching, Germany.
Nico StrohmeyerDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule Zürich, Basel, Switzerland.ORCID 0000-0002-5985-9800
Michael SattlerDepartment of Bioscience, Technical University of Munich, TUM School of Natural Sciences, Garching, Germany.
Reinhard FässlerDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried, Germany. faessler@biochem.mpg.de.ORCID 0000-0002-0145-6937
Helmholtz Zentrum München · DEMax Planck Institute of Biochemistry · DEBoard of the Swiss Federal Institutes of Technology · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrin affinity regulation, also termed integrin activation, is essential for metazoan life. Although talin and kindlin binding to the β-integrin cytoplasmic tail is indispensable for integrin activation, it is unknown how they achieve this function. By combining NMR, biochemistry and cell biology techniques, we found that talin and kindlin binding to the β-tail can induce a conformational change that increases talin affinity and decreases kindlin affinity toward it. We also discovered that this asymmetric affinity regulation is accompanied by a direct interaction between talin and kindlin, which promotes simultaneous binding of talin and kindlin to β-tails. Disrupting allosteric communication between the β-tail-binding sites of talin and kindlin or their direct interaction in cells severely compromised integrin functions. These data show how talin and kindlin cooperate to generate a small but critical population of ternary talin-β-integrin-kindlin complexes with high talin-integrin affinity and high dynamics.

Indexed as

IntegrinsTalinAnimalsBinding SitesProtein BindingIntegrinsTalin

Identifiers

PMID38087085
PMCPMC10716038
OpenAlexW4389612585

What OpenQuestion holds

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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.