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Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization
Classical cadherin adhesion molecules are key determinants of cell–cell recognition during development and in post-embryonic life. A decisive step in productive cadherin-based recognition is the conversion of nascent adhesions into stable zones of contact. It is increasingly clear that such contact...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2004
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172285/ https://www.ncbi.nlm.nih.gov/pubmed/15024035 http://dx.doi.org/10.1083/jcb.200309034 |
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author | Helwani, Falak M. Kovacs, Eva M. Paterson, Andrew D. Verma, Suzie Ali, Radiya G. Fanning, Alan S. Weed, Scott A. Yap, Alpha S. |
author_facet | Helwani, Falak M. Kovacs, Eva M. Paterson, Andrew D. Verma, Suzie Ali, Radiya G. Fanning, Alan S. Weed, Scott A. Yap, Alpha S. |
author_sort | Helwani, Falak M. |
collection | PubMed |
description | Classical cadherin adhesion molecules are key determinants of cell–cell recognition during development and in post-embryonic life. A decisive step in productive cadherin-based recognition is the conversion of nascent adhesions into stable zones of contact. It is increasingly clear that such contact zone extension entails active cooperation between cadherin adhesion and the force-generating capacity of the actin cytoskeleton. Cortactin has recently emerged as an important regulator of actin dynamics in several forms of cell motility. We now report that cortactin is recruited to cell–cell adhesive contacts in response to homophilic cadherin ligation. Notably, cortactin accumulates preferentially, with Arp2/3, at cell margins where adhesive contacts are being extended. Recruitment of cortactin is accompanied by a ligation-dependent biochemical interaction between cortactin and the cadherin adhesive complex. Inhibition of cortactin activity in cells blocked Arp2/3-dependent actin assembly at cadherin adhesive contacts, significantly reduced cadherin adhesive contact zone extension, and perturbed both cell morphology and junctional accumulation of cadherins in polarized epithelia. Together, our findings identify a necessary role for cortactin in the cadherin–actin cooperation that supports productive contact formation. |
format | Text |
id | pubmed-2172285 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21722852008-03-05 Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization Helwani, Falak M. Kovacs, Eva M. Paterson, Andrew D. Verma, Suzie Ali, Radiya G. Fanning, Alan S. Weed, Scott A. Yap, Alpha S. J Cell Biol Article Classical cadherin adhesion molecules are key determinants of cell–cell recognition during development and in post-embryonic life. A decisive step in productive cadherin-based recognition is the conversion of nascent adhesions into stable zones of contact. It is increasingly clear that such contact zone extension entails active cooperation between cadherin adhesion and the force-generating capacity of the actin cytoskeleton. Cortactin has recently emerged as an important regulator of actin dynamics in several forms of cell motility. We now report that cortactin is recruited to cell–cell adhesive contacts in response to homophilic cadherin ligation. Notably, cortactin accumulates preferentially, with Arp2/3, at cell margins where adhesive contacts are being extended. Recruitment of cortactin is accompanied by a ligation-dependent biochemical interaction between cortactin and the cadherin adhesive complex. Inhibition of cortactin activity in cells blocked Arp2/3-dependent actin assembly at cadherin adhesive contacts, significantly reduced cadherin adhesive contact zone extension, and perturbed both cell morphology and junctional accumulation of cadherins in polarized epithelia. Together, our findings identify a necessary role for cortactin in the cadherin–actin cooperation that supports productive contact formation. The Rockefeller University Press 2004-03-15 /pmc/articles/PMC2172285/ /pubmed/15024035 http://dx.doi.org/10.1083/jcb.200309034 Text en Copyright © 2004, The Rockefeller University Press 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 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Helwani, Falak M. Kovacs, Eva M. Paterson, Andrew D. Verma, Suzie Ali, Radiya G. Fanning, Alan S. Weed, Scott A. Yap, Alpha S. Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization |
title | Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization |
title_full | Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization |
title_fullStr | Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization |
title_full_unstemmed | Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization |
title_short | Cortactin is necessary for E-cadherin–mediated contact formation and actin reorganization |
title_sort | cortactin is necessary for e-cadherin–mediated contact formation and actin reorganization |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172285/ https://www.ncbi.nlm.nih.gov/pubmed/15024035 http://dx.doi.org/10.1083/jcb.200309034 |
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