Myosin light chain kinase: An actin-binding protein that regulates an ATP-dependent interaction with myosin

被引:53
|
作者
Kohama, K
Ye, LH
Hayakawa, K
Okagaki, T
机构
[1] Department of Pharmacology, Gunma University School of Medicine, Maebashi
关键词
D O I
10.1016/0165-6147(96)10033-X
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Myosin light chain kinase (MLCK) is a key regulator of smooth muscle contraction. The most conspicuous form of regulation is achieved by phosphorylation of the myosin light chain, allowing myosin to interact with actin. This interaction is regulated by actin-binding proteins that modulate actin filaments. In this review Kazuhiro Kohama and colleagues consider MLCK as an actin-binding protein and attempt to shed light on the cross-talk between the different kinds of regulation of the actin-myosin interaction in smooth muscle. An understanding of these mechanisms will assist the development of compounds with therapeutic importance in muscular disorders.
引用
收藏
页码:284 / 287
页数:4
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