Open AccessCellular tension encodes local Src-dependent differential β1 and β3 integrin mobility
Author(s) -
Richard De Mets,
Irène Wang,
Martial Balland,
Christiane Oddou,
Philippe Moreau,
B. Fourcade,
Corinne Albiges-Rizo,
Antoine Delon,
Olivier Destaing
Publication year - 2019
Publication title -
molecular biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.463
H-Index - 225
eISSN - 1939-4586
pISSN - 1059-1524
DOI - 10.1091/mbc.e18-04-0253
Subject(s) - integrin , microbiology and biotechnology , biology , mechanotransduction , cytoskeleton , proto oncogene tyrosine protein kinase src , cell adhesion , focal adhesion , collagen receptor , biophysics , phosphorylation , receptor , cell , biochemistry
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.