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Published online June 16, 2008
doi:10.1083/jcb.200710187
The Journal of Cell Biology, Vol. 181, No. 6, 999-1012
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Lee et al.
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Article

 Regulation of RhoA-dependent ROCKII activation by Shp2

Hsiao-Hui Lee and Zee-Fen Chang

Institute of Biochemistry and Molecular Biology, College of Medicine, National Taiwan University, Taipei 100, Taiwan

Correspondence to Zee-Fen Chang: zfchang{at}ntu.edu.tw

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.

Abbreviations used in this paper: FN, fibronectin; MLC, myosin light chain; PTP, protein tyrosine phosphatase; RBD, rho binding domain; ROCK, rho kinase; SRE, serum-responsive element; SRF, serum response factor.


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