Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase

被引：181

作者：

Koyama, M

Ito, M ^{[1
]}

Feng, JH

Seko, T

Shiraki, K

Takase, K

Hartshorne, DJ

Nakano, T

机构：

[1] Mie Univ, Sch Med, Dept Internal Med 1, Tsu, Mie 5148507, Japan

[2] Univ Arizona, Muscle Biol Grp, Tucson, AZ 85721 USA

来源：

FEBS LETTERS | 2000年 / 475卷 / 03期

关键词：

Rho-kinase; myosin phosphatase; CPI-17; smooth muscle; Ca2+ sensitization;

D O I：

10.1016/S0014-5793(00)01654-9

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：

Phosphorylation of CPI-17 by Rho-associated kinase (Rho-kinase) and its effect on myosin phosphatase (MP) activity were investigated. CPI-17 was phosphorylated by Rho-kinase to 0.92 mol of P/mol of CPI-17 in vitro. The inhibitory phosphorylation site was Thr(38) (as reported previously) and was identified using a point mutant of CPI-17 and a phosphorylation state-specific antibody. Phosphorylation by Rho-kinase dramatically increased the inhibitory effect of CPI-17 on MP activity. Thus, CPI-17 as a substrate of Rho-kinase could be involved in the Ca2+ sensitization of smooth muscle contraction as a downstream effector of Rho-kinase. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

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页码：197 / 200

页数：4

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