Regulation of myosin phosphatase by Rho and Rho-Associated kinase (Rho-kinase)

被引：2415

作者：

Kimura, K

Ito, M

Amano, M

Chihara, K

Fukata, Y

Nakafuku, M

Yamamori, B

Feng, JH

Nakano, T

Okawa, K

Iwamatsu, A

Kaibuchi, K

机构：

[1] NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT,IKOMA 63001,JAPAN

[2] MIE UNIV,SCH MED,DEPT INTERNAL MED 1,TSU,MIE 514,JAPAN

[3] KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,YOKOHAMA,KANAGAWA 236,JAPAN

来源：

SCIENCE | 1996年 / 273卷 / 5272期

关键词：

D O I：

10.1126/science.273.5272.245

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP . RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP . RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.

引用

页码：245 / 248

页数：4

共 32 条

[1] Identification of a putative target for Rho as the serine-threonine kinase protein kinase N [J].