title: [Activation of smooth muscle myosin by the non-kinase role of myosin light chain kinase].
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.
authors.affiliation: Department of Pharmacology, Gunma University School of Medicine, Gunma 371-8511, Japan.
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Kohama
mesh_terms: D000818:Animals; D009119:Muscle Contraction; D009130:Muscle, Smooth / Q000502:physiology*; D009219:Myosin-Light-Chain Kinase / Q000502:physiology*; D009218:Myosins / Q000378:metabolism*; D010766:Phosphorylation
chemical_list: D009219:Myosin-Light-Chain Kinase; D009218:Myosins