期刊
JOURNAL OF CELL BIOLOGY
卷 217, 期 11, 页码 3776-3784出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201808061
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资金
- Biotechnology and Biological Sciences Research Council [BB/N007336/1]
- National Research Foundation (NRF), Prime Minister's Office, Singapore, under its NRF Investigatorship Program (NRF Investigatorship Award) [NRF-NRFI2016-03]
- Human Frontier Science Program [RGP00001/2016]
- Biotechnology and Biological Sciences Research Council [BB/N007336/1] Funding Source: researchfish
- BBSRC [BB/N007336/1] Funding Source: UKRI
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 alpha-helical bundles that form its long rod domain. Talin binds to the cytoplasmic domain of integrin beta-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.
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