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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...

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Autores principales: Helwani, Falak M., Kovacs, Eva M., Paterson, Andrew D., Verma, Suzie, Ali, Radiya G., Fanning, Alan S., Weed, Scott A., Yap, Alpha S.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2004
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.
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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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