title: Myosin light chain kinase: an actin-binding protein that regulates an ATP-dependent interaction with myosin.
abstract: Myosin light chain kinase (MLCK) is a key regulator of smooth muscle contraction. The most conspicuous form of regulation is achieved by phosphorylation of the myosin light chain, allowing myosin to interact with actin. This interaction is regulated by actin-binding proteins that modulate actin filaments. In this review Kazuhiro Kohama and colleagues consider MLCK as an actin-binding protein and attempt to shed light on the cross-talk between the different kinds of regulation of the actin-myosin interaction in smooth muscle. An understanding of these mechanisms will assist the development of compounds with therapeutic importance in muscular disorders.
authors.affiliation: Department of Pharmacology, Gunma University School of Medicine, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Kohama
authors.forename: L H
authors.initials: LH
authors.lastname: Ye
authors.forename: K
authors.initials: K
authors.lastname: Hayakawa
authors.forename: T
authors.initials: T
authors.lastname: Okagaki
mesh_terms: D000199:Actins / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000502:physiology*; D000818:Animals; D006801:Humans; D009219:Myosin-Light-Chain Kinase / Q000502:physiology*; D009218:Myosins / Q000502:physiology*; D011485:Protein Binding
chemical_list: D000199:Actins; D000255:Adenosine Triphosphate; D009219:Myosin-Light-Chain Kinase; D009218:Myosins