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FAK promotes recruitment of talin to nascent adhesions to control cell motility
Cell migration is a dynamic process that involves the continuous formation, maturation, and turnover of matrix–cell adhesion sites. New (nascent) adhesions form at the protruding cell edge in a tension-independent manner and are comprised of integrin receptors, signaling, and cytoskeletal-associated...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265949/ https://www.ncbi.nlm.nih.gov/pubmed/22270917 http://dx.doi.org/10.1083/jcb.201108078 |
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author | Lawson, Christine Lim, Ssang-Taek Uryu, Sean Chen, Xiao Lei Calderwood, David A. Schlaepfer, David D. |
author_facet | Lawson, Christine Lim, Ssang-Taek Uryu, Sean Chen, Xiao Lei Calderwood, David A. Schlaepfer, David D. |
author_sort | Lawson, Christine |
collection | PubMed |
description | Cell migration is a dynamic process that involves the continuous formation, maturation, and turnover of matrix–cell adhesion sites. New (nascent) adhesions form at the protruding cell edge in a tension-independent manner and are comprised of integrin receptors, signaling, and cytoskeletal-associated proteins. Integrins recruit focal adhesion kinase (FAK) and the cytoskeletal protein talin to nascent adhesions. Canonical models support a role for talin in mediating FAK localization and activation at adhesions. Here, alternatively, we show that FAK promotes talin recruitment to nascent adhesions occurring independently of talin binding to β1 integrins. The direct binding site for talin on FAK was identified, and a point mutation in FAK (E1015A) prevented talin association and talin localization to nascent adhesions but did not alter integrin-mediated FAK recruitment and activation at adhesions. Moreover, FAK E1015A inhibited cell motility and proteolytic talin cleavage needed for efficient adhesion dynamics. These results support an alternative linkage for FAK–talin interactions within nascent adhesions essential for the control of cell migration. |
format | Online Article Text |
id | pubmed-3265949 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-32659492012-07-23 FAK promotes recruitment of talin to nascent adhesions to control cell motility Lawson, Christine Lim, Ssang-Taek Uryu, Sean Chen, Xiao Lei Calderwood, David A. Schlaepfer, David D. J Cell Biol Research Articles Cell migration is a dynamic process that involves the continuous formation, maturation, and turnover of matrix–cell adhesion sites. New (nascent) adhesions form at the protruding cell edge in a tension-independent manner and are comprised of integrin receptors, signaling, and cytoskeletal-associated proteins. Integrins recruit focal adhesion kinase (FAK) and the cytoskeletal protein talin to nascent adhesions. Canonical models support a role for talin in mediating FAK localization and activation at adhesions. Here, alternatively, we show that FAK promotes talin recruitment to nascent adhesions occurring independently of talin binding to β1 integrins. The direct binding site for talin on FAK was identified, and a point mutation in FAK (E1015A) prevented talin association and talin localization to nascent adhesions but did not alter integrin-mediated FAK recruitment and activation at adhesions. Moreover, FAK E1015A inhibited cell motility and proteolytic talin cleavage needed for efficient adhesion dynamics. These results support an alternative linkage for FAK–talin interactions within nascent adhesions essential for the control of cell migration. The Rockefeller University Press 2012-01-23 /pmc/articles/PMC3265949/ /pubmed/22270917 http://dx.doi.org/10.1083/jcb.201108078 Text en © 2012 Lawson et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Lawson, Christine Lim, Ssang-Taek Uryu, Sean Chen, Xiao Lei Calderwood, David A. Schlaepfer, David D. FAK promotes recruitment of talin to nascent adhesions to control cell motility |
title | FAK promotes recruitment of talin to nascent adhesions to control cell motility |
title_full | FAK promotes recruitment of talin to nascent adhesions to control cell motility |
title_fullStr | FAK promotes recruitment of talin to nascent adhesions to control cell motility |
title_full_unstemmed | FAK promotes recruitment of talin to nascent adhesions to control cell motility |
title_short | FAK promotes recruitment of talin to nascent adhesions to control cell motility |
title_sort | fak promotes recruitment of talin to nascent adhesions to control cell motility |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3265949/ https://www.ncbi.nlm.nih.gov/pubmed/22270917 http://dx.doi.org/10.1083/jcb.201108078 |
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