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 Lifejournal_title
IUBMB lifeauthors
Gao Y,Ye LH,Kishi H,Okagaki T,Samizo K,Nakamura A,Kohama Kdoi
10.1080/152165401753366087keywords:
subject
Has Abstractpub_date
2001-06-01 00:00:00pages
337-44issue
6eissn
1521-6543issn
1521-6551journal_volume
51pub_type
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