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[Activation of smooth muscle myosin by the non-kinase role of myosin light chain kinase].

Authors
Type
Published Article
Journal
Nihon yakurigaku zasshi. Folia pharmacologica Japonica
Publication Date
Volume
122 Suppl
Identifiers
PMID: 14727523
Source
Medline
License
Unknown

Abstract

Myosin light chain kinase (MLCK) is a regulatory protein for smooth muscle contraction, which acts by phosphorylating 20-kDa myosin light chain (MLLC20) to activate the myosin ATPase activity. Although this mode of action is well-established, there are numberous 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. I will overview 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 and migration.

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