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

被引：165

作者：

Velasco, G

Armstrong, C

Morrice, N

Frame, S

Cohen, P ^{[1
]}

机构：

[1] Univ Dundee, Div Signal Transduct Therapy, Sch Life Sci, Dundee DD1 5EH, Scotland

[2] Univ Dundee, MRC, Sch Life Sci, Prot Phosphorylat Unit, Dundee DD1 5EH, Scotland

[3] Univ Complutense, Dept Biochem & Mol Biol 1, Sch Biol, E-28040 Madrid, Spain

[4] Upstate Ltd, Dundee DD2 1SW, Scotland

[5] Cyclacel, Dundee Technopole, Dundee DD1 5JJ, Scotland

来源：

FEBS LETTERS | 2002年 / 527卷 / 1-3期

基金：

英国医学研究理事会;

关键词：

protein phosphatase 1; Rho kinase; smooth muscle; myosin;

D O I：

10.1016/S0014-5793(02)03175-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：101 / 104

页数：4

共 22 条

[21] THE PROTEIN PHOSPHATASES INVOLVED IN CELLULAR-REGULATION - PURIFICATION AND CHARACTERIZATION OF THE GLYCOGEN-BOUND FORM OF PROTEIN PHOSPHATASE-1 FROM RABBIT SKELETAL-MUSCLE [J].