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Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin
Authors:Velasco Guillermo  Armstrong Chris  Morrice Nick  Frame Sheelagh  Cohen Philip
Institution:Division of Signal Transduction Therapy, School of Life Sciences, University of Dundee, DD1 5EH, Dundee, UK.
Abstract: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.
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