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Mol Biol Cell. 2019 Jan 15;30(2):181-190. doi: 10.1091/mbc.E18-04-0253. Epub 2018 Nov 21.

Cellular tension encodes local Src-dependent differential β1 and β3 integrin mobility.

Author information

1
Laboratoire interdisciplinaire de Physique, Université Grenoble Alpes et CNRS, 38402 Grenoble, Cedex, France.
2
Institut Albert Bonniot, Université Joseph Fourier, INSERM U823, CNRS ERL 5284, Grenoble Alpessite Santé, F38042 Grenoble Cedex 09, France.

Abstract

Integrins are transmembrane receptors that have a pivotal role in mechanotransduction processes by connecting the extracellular matrix to the cytoskeleton. Although it is well established that integrin activation/inhibition cycles are due to highly dynamic interactions, whether integrin mobility depends on local tension and cytoskeletal organization remains surprisingly unclear. Using an original approach combining micropatterning on glass substrates to induce standardized local mechanical constraints within a single cell with temporal image correlation spectroscopy, we measured the mechanosensitive response of integrin mobility at the whole cell level and in adhesion sites under different mechanical constraints. Contrary to β1 integrins, high tension increases β3 integrin residence time in adhesive regions. Chimeric integrins and structure-function studies revealed that the ability of β3 integrins to specifically sense local tensional organization is mostly encoded by its cytoplasmic domain and is regulated by tuning the affinity of its NPXY domains through phosphorylation by Src family kinases.

PMID:
30462575
DOI:
10.1091/mbc.E18-04-0253

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