Evidence map›Paper›PMID 37339195›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Kindlin stabilizes the talin·integrin bond under mechanical load by generating an ideal bond.

Mihai Adrian Bodescu, Jonas Aretz, Marco Grison, Matthias Rief, Reinhard Fässler

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

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  8. Compressed Cells Facilitate Adhesion Through Glycocalyx.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  10. Kindlin Regulates Mechanosensitive Activation and Adhesion Assembly of Integrin beta6.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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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 2 institutions in 1 country.

Mihai Adrian BodescuCenter for Protein Assemblies and TUM School of Natural Sciences, Department of Bioscience, Chair of Molecular Biophysics, Technical University of Munich, Garching 85748, Germany.
Jonas AretzDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.ORCID 0000-0002-4623-5820
Marco GrisonCenter for Protein Assemblies and TUM School of Natural Sciences, Department of Bioscience, Chair of Molecular Biophysics, Technical University of Munich, Garching 85748, Germany.
Matthias RiefCenter for Protein Assemblies and TUM School of Natural Sciences, Department of Bioscience, Chair of Molecular Biophysics, Technical University of Munich, Garching 85748, Germany.
Reinhard FässlerDepartment of Molecular Medicine, Max Planck Institute of Biochemistry, Martinsried 82152, Germany.
Technical University of Munich · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrin-mediated adhesion is essential for metazoan life. Integrin binding to ligand requires an activation step prior to binding ligand that depends on direct binding of talin and kindlin to the β-integrin cytoplasmic tail and the transmission of force from the actomyosin via talin to the integrin-ligand bonds. However, the affinity of talin for integrin tails is low. It is therefore still unclear how such low-affinity bonds are reinforced to transmit forces up to 10 to 40 pN. In this study, we use single-molecule force spectroscopy by optical tweezers to investigate the mechanical stability of the talin•integrin bond in the presence and absence of kindlin. While talin and integrin alone form a weak and highly dynamic slip bond, the addition of kindlin-2 induces a force-independent, ideal talin•integrin bond, which relies on the steric proximity of and the intervening amino acid sequences between the talin- and kindlin-binding sites in the β-integrin tail. Our findings show how kindlin cooperates with talin to enable transmission of high forces required to stabilize cell adhesion.

Indexed as

IntegrinsTalinAnimalsCell AdhesionLigandsMembrane ProteinsIntegrinsLigandsMembrane ProteinsTalinfocal adhesionideal bondintegrinsoptical tweezerssingle-molecule

Identifiers

PMID37339195
PMCPMC10293852
OpenAlexW4381435896

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.