Journal
FEBS LETTERS
Volume 527, Issue 1-3, Pages 101-104Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03175-7
Keywords
protein phosphatase 1; Rho kinase; smooth muscle; myosin
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Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited. (C) 2002 Federation of European Biochemical Societies.
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