Dephosphorylation of distinct sites on the 20 kDa myosin light chain by smooth muscle myosin phosphatase

被引：11

作者：

Feng, JH

Ito, M ^{[1
]}

Nishikawa, M

Okinaka, T

Isaka, N

Hartshorne, DJ

Nakano, T

机构：

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

[2] Mie Univ, Sch Med, Dept Internal Med 2, Tsu, Mie 5148507, Japan

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

来源：

FEBS LETTERS | 1999年 / 448卷 / 01期

关键词：

smooth muscle myosin; myosin light chain; myosin phosphatase; myosin light chain kinase; protein kinase C;

D O I：

10.1016/S0014-5793(99)00337-3

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：

The dephosphorylation of the myosin light chain kinase and protein kinase C sites on the 20 kDa myosin light chain by myosin phosphatase was investigated. The myosin phosphatase holoenzyme and catalytic subunit, dephosphorylated Ser-19, Thr-18 and Thr-9, but not Ser-1/Ser-2, The role of noncatalytic subunits in myosin phosphatase mas to activate the phosphatase activity. For Ser-19 and Thr-18, this was due to a decrease in K-m and an increase in k(cat) and for Thr-9 to a decrease in K-m. Thus, the distinction between the various sites is a property of the catalytic subunit, (C) 1999 Federation of European Biochemical Societies.

引用

页码：101 / 104

页数：4

共 40 条

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