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Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility

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 dep...

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Autores principales: De Mets, Richard, Wang, Irene, Balland, Martial, Oddou, Christiane, Moreau, Philippe, Fourcade, Bertrand, Albiges-Rizo, Corinne, Delon, Antoine, Destaing, Olivier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6589565/
https://www.ncbi.nlm.nih.gov/pubmed/30462575
http://dx.doi.org/10.1091/mbc.E18-04-0253
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author De Mets, Richard
Wang, Irene
Balland, Martial
Oddou, Christiane
Moreau, Philippe
Fourcade, Bertrand
Albiges-Rizo, Corinne
Delon, Antoine
Destaing, Olivier
author_facet De Mets, Richard
Wang, Irene
Balland, Martial
Oddou, Christiane
Moreau, Philippe
Fourcade, Bertrand
Albiges-Rizo, Corinne
Delon, Antoine
Destaing, Olivier
author_sort De Mets, Richard
collection PubMed
description 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.
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spelling pubmed-65895652019-06-28 Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility De Mets, Richard Wang, Irene Balland, Martial Oddou, Christiane Moreau, Philippe Fourcade, Bertrand Albiges-Rizo, Corinne Delon, Antoine Destaing, Olivier Mol Biol Cell Brief Reports 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. The American Society for Cell Biology 2019-01-15 /pmc/articles/PMC6589565/ /pubmed/30462575 http://dx.doi.org/10.1091/mbc.E18-04-0253 Text en © 2019 De Mets et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0 This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License.
spellingShingle Brief Reports
De Mets, Richard
Wang, Irene
Balland, Martial
Oddou, Christiane
Moreau, Philippe
Fourcade, Bertrand
Albiges-Rizo, Corinne
Delon, Antoine
Destaing, Olivier
Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility
title Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility
title_full Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility
title_fullStr Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility
title_full_unstemmed Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility
title_short Cellular tension encodes local Src-dependent differential β(1) and β(3) integrin mobility
title_sort cellular tension encodes local src-dependent differential β(1) and β(3) integrin mobility
topic Brief Reports
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6589565/
https://www.ncbi.nlm.nih.gov/pubmed/30462575
http://dx.doi.org/10.1091/mbc.E18-04-0253
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