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J Cell Biol. 2018 Nov 5;217(11):3776-3784. doi: 10.1083/jcb.201808061. Epub 2018 Sep 25.

Talin as a mechanosensitive signaling hub.

Author information

1
School of Biosciences, University of Kent, Canterbury, UK b.t.goult@kent.ac.uk.
2
Mechanobiology Institute, National University of Singapore, Singapore.
3
Department of Physics, National University of Singapore, Singapore.
4
Centre for Bioimaging Sciences, National University of Singapore, Singapore.
5
Wellcome Trust Centre for Matrix Research, University of Manchester, Manchester, UK.
6
Yale Cardiovascular Research Center and Departments of Internal Medicine (Cardiology), Cell Biology, and Biomedical Engineering, Yale School of Medicine, New Haven, CT.

Abstract

Cell adhesion to the extracellular matrix (ECM), mediated by transmembrane receptors of the integrin family, is exquisitely sensitive to biochemical, structural, and mechanical features of the ECM. Talin is a cytoplasmic protein consisting of a globular head domain and a series of α-helical bundles that form its long rod domain. Talin binds to the cytoplasmic domain of integrin β-subunits, activates integrins, couples them to the actin cytoskeleton, and regulates integrin signaling. Recent evidence suggests switch-like behavior of the helix bundles that make up the talin rod domains, where individual domains open at different tension levels, exerting positive or negative effects on different protein interactions. These results lead us to propose that talin functions as a mechanosensitive signaling hub that integrates multiple extracellular and intracellular inputs to define a major axis of adhesion signaling.

PMID:
30254032
PMCID:
PMC6219721
[Available on 2019-05-05]
DOI:
10.1083/jcb.201808061

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