Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin

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, w...

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Veröffentlicht in:	FEBS letters 2002-09, Vol.527 (1-3), p.101-104
Hauptverfasser:	Velasco, Guillermo, Armstrong, Chris, Morrice, Nick, Frame, Sheelagh, Cohen, Philip
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Base Sequence Catalytic Domain Intracellular Signaling Peptides and Proteins Molecular Sequence Data Muscle, Smooth - metabolism Myosin Myosin-Light-Chain Phosphatase Myosins - metabolism MYPT1, myosin phosphatase targetting 1 Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism Phosphorylation PP1, protein phosphatase 1 PP1C, protein phosphatase 1 catalytic subunit PP1M, smooth muscle protein phosphatase 1 Protein Phosphatase 1 Protein Subunits Protein-Serine-Threonine Kinases - metabolism Rho kinase rho-Associated Kinases ROKα/ROCK-II, Rho-dependent protein kinase Smooth muscle Threonine - metabolism
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Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(02)03175-7