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Myosin Light Chain Kinase as a Multifunctional Regulatory Protein of Smooth Muscle Contraction
Author(s) -
Gao Ying,
Ye LiHong,
Kishi Hiroko,
Okagaki Tsuyoshi,
Samizo Koichi,
Nakamura Akio,
Kohama Kazuhiro
Publication year - 2001
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/152165401753366087
Subject(s) - myosin light chain kinase , myosin , phosphorylation , meromyosin , actin , myh7 , contraction (grammar) , rho associated protein kinase , microbiology and biotechnology , muscle contraction , immunoglobulin light chain , biochemistry , chemistry , biology , myosin head , anatomy , endocrinology , antibody , immunology
Myosin light chain kinase (MLCK) is a regulatory protein for smooth muscle contraction, which acts by phosphorylating 20‐kDa myosin light chain (MLC20) to activate the myosin ATPase activity. Although this mode of action is well‐established, there are numerous reports of smooth muscle contraction that is not associated with MLC20 phosphorylation. The kinase activity for the phosphorylation is localized at the central part of MLCK, which is also furnished with actin‐binding activity at its N terminal and myosin‐binding activity at its C terminal. This article overviews as to how such multifunctional properties of MLCK modify the actin‐myosin interaction and presents our observations that the phosphorylation is not obligatory in induction of smooth muscle contraction.