Myosin light chain kinase as a multifunctional regulatory protein of smooth muscle contraction.

Abstract:

: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.

journal_name

IUBMB Life

journal_title

IUBMB life

authors

Gao Y,Ye LH,Kishi H,Okagaki T,Samizo K,Nakamura A,Kohama K

doi

10.1080/152165401753366087

keywords:

subject

Has Abstract

pub_date

2001-06-01 00:00:00

pages

337-44

issue

6

eissn

1521-6543

issn

1521-6551

journal_volume

51

pub_type

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