Evidence map›Paper›PMID 27548916›Full record

ArticleNature cell biology2016

Kank2 activates talin, reduces force transduction across integrins and induces central adhesion formation.

Zhiqi Sun, Hui-Yuan Tseng, Steven Tan, Fabrice Senger, Laetitia Kurzawa, Dirk Dedden, Naoko Mizuno, Anita A Wasik, Manuel Thery, Alexander R Dunn and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 2 pooled it
11.2field-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

92 citing papers in PubMed, 2 syntheses or guidelines pooled it, 179 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Review
  5. ILK binding to β1 integrin is indirect and mediated by kindlin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Synergistic effect of PIPBiophysical journal · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. The role and regulation of integrins in cell migration and invasion.Nature reviews. Molecular cell biology · 2025
    Review
  18. Article
  19. Article
  20. Review

32 more citing papers are in PubMed but not listed here.

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 5 institutions in 3 countries.

Zhiqi SunMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Hui-Yuan TsengMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Steven TanDepartment of Chemical Engineering, Stanford University, Stanford, California 94305, USA.
Fabrice SengerCytoMorpho Lab, Biosciences &Biotechnology Institute of Grenoble, UMR5168, CEA/INRA/CNRS/Université, 38054 Grenoble-Alpes, Grenoble, France.
Laetitia KurzawaCytoMorpho Lab, Biosciences &Biotechnology Institute of Grenoble, UMR5168, CEA/INRA/CNRS/Université, 38054 Grenoble-Alpes, Grenoble, France.
Dirk DeddenMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Naoko MizunoMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Anita A WasikMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Manuel TheryCytoMorpho Lab, Biosciences &Biotechnology Institute of Grenoble, UMR5168, CEA/INRA/CNRS/Université, 38054 Grenoble-Alpes, Grenoble, France.
Alexander R DunnDepartment of Chemical Engineering, Stanford University, Stanford, California 94305, USA.
Reinhard FässlerMax Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Max Planck Institute of Biochemistry · DELaboratoire Physiologie Cellulaire & Végétale · FRCEA Grenoble · FRFranciscan University of Steubenville · USStanford University · US

Funding

Biophysical mechanisms of mechanical tension sensing at cellular integrin complexesR01GM112998 · NIGMS · STANFORD UNIVERSITY · PI DUNN, ALEXANDER R · 2015 to 2018
$1.3M
NIGMS NIH HHS R01 GM112998
6 · The paper itself

Abstract

Integrin-based adhesions play critical roles in cell migration. Talin activates integrins and flexibly connects integrins to the actomyosin cytoskeleton, thereby serving as a 'molecular clutch' that transmits forces to the extracellular matrix to drive cell migration. Here we identify the evolutionarily conserved Kank protein family as novel components of focal adhesions (FAs). Kank proteins accumulate at the lateral border of FAs, which we term the FA belt, and in central sliding adhesions, where they directly bind the talin rod domain through the Kank amino-terminal (KN) motif and induce talin and integrin activation. In addition, Kank proteins diminish the talin-actomyosin linkage, which curbs force transmission across integrins, leading to reduced integrin-ligand bond strength, slippage between integrin and ligand, central adhesion formation and sliding, and reduced cell migration speed. Our data identify Kank proteins as talin activators that decrease the grip between the integrin-talin complex and actomyosin to regulate cell migration velocity.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCell AdhesionCell MembraneCell MovementCells, CulturedCytoskeletal ProteinsCytoskeletonExtracellular MatrixFocal AdhesionsIntegrinsMiceTalinVinculinAdaptor Proteins, Signal TransducingCarrier ProteinsCytoskeletal ProteinsIntegrinsKank1 protein, mouseTalinVinculin

Identifiers

PMID27548916
PMCPMC6053543
OpenAlexW2511488239

What OpenQuestion holds

Textmetadata
LicenceTDM
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.