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Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin
Author(s) -
Velasco Guillermo,
Armstrong Chris,
Morrice Nick,
Frame Sheelagh,
Cohen Philip
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03175-7
Subject(s) - myosin , phosphorylation , phosphatase , myosin light chain kinase , protein subunit , myosin light chain phosphatase , dephosphorylation , microbiology and biotechnology , protein kinase a , kinase , contractility , protein phosphatase 1 , chemistry , biochemistry , biology , endocrinology , gene
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.