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Regulation of RhoA-dependent ROCKII activation by Shp2

Contractile forces mediated by RhoA and Rho kinase (ROCK) are required for a variety of cellular processes, including cell adhesion. In this study, we show that RhoA-dependent ROCKII activation is negatively regulated by phosphorylation at a conserved tyrosine residue (Y722) in the coiled-coil domai...

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Detalles Bibliográficos
Autores principales: Lee, Hsiao-Hui, Chang, Zee-Fen
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2008
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2426933/
https://www.ncbi.nlm.nih.gov/pubmed/18559669
http://dx.doi.org/10.1083/jcb.200710187
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author Lee, Hsiao-Hui
Chang, Zee-Fen
author_facet Lee, Hsiao-Hui
Chang, Zee-Fen
author_sort Lee, Hsiao-Hui
collection PubMed
description Contractile forces mediated by RhoA and Rho kinase (ROCK) are required for a variety of cellular processes, including cell adhesion. In this study, we show that RhoA-dependent ROCKII activation is negatively regulated by phosphorylation at a conserved tyrosine residue (Y722) in the coiled-coil domain of ROCKII. Tyrosine phosphorylation of ROCKII is increased with cell adhesion, and loss of Y722 phosphorylation delays adhesion and spreading on fibronectin, suggesting that this modification is critical for restricting ROCKII-mediated contractility during these processes. Further, we provide evidence that Shp2 mediates dephosphorylation of ROCKII and, therefore, regulates RhoA-induced cell rounding, indicating that Shp2 couples with RhoA signaling to control ROCKII activation during deadhesion. Thus, reversible tyrosine phosphorylation confers an additional layer of control to fine-tune RhoA-dependent activation of ROCKII.
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spelling pubmed-24269332008-12-16 Regulation of RhoA-dependent ROCKII activation by Shp2 Lee, Hsiao-Hui Chang, Zee-Fen J Cell Biol Research Articles Contractile forces mediated by RhoA and Rho kinase (ROCK) are required for a variety of cellular processes, including cell adhesion. In this study, we show that RhoA-dependent ROCKII activation is negatively regulated by phosphorylation at a conserved tyrosine residue (Y722) in the coiled-coil domain of ROCKII. Tyrosine phosphorylation of ROCKII is increased with cell adhesion, and loss of Y722 phosphorylation delays adhesion and spreading on fibronectin, suggesting that this modification is critical for restricting ROCKII-mediated contractility during these processes. Further, we provide evidence that Shp2 mediates dephosphorylation of ROCKII and, therefore, regulates RhoA-induced cell rounding, indicating that Shp2 couples with RhoA signaling to control ROCKII activation during deadhesion. Thus, reversible tyrosine phosphorylation confers an additional layer of control to fine-tune RhoA-dependent activation of ROCKII. The Rockefeller University Press 2008-06-16 /pmc/articles/PMC2426933/ /pubmed/18559669 http://dx.doi.org/10.1083/jcb.200710187 Text en © 2008 Lee and Chang 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.jcb.org/misc/terms.shtml). 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
Lee, Hsiao-Hui
Chang, Zee-Fen
Regulation of RhoA-dependent ROCKII activation by Shp2
title Regulation of RhoA-dependent ROCKII activation by Shp2
title_full Regulation of RhoA-dependent ROCKII activation by Shp2
title_fullStr Regulation of RhoA-dependent ROCKII activation by Shp2
title_full_unstemmed Regulation of RhoA-dependent ROCKII activation by Shp2
title_short Regulation of RhoA-dependent ROCKII activation by Shp2
title_sort regulation of rhoa-dependent rockii activation by shp2
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2426933/
https://www.ncbi.nlm.nih.gov/pubmed/18559669
http://dx.doi.org/10.1083/jcb.200710187
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