Phosphorylation of smooth muscle myosin light chain kinase by protein kinase C. Comparative study of the phosphorylated sites.
作者： M Nishikawa , S Shirakawa , R S Adelstein
DOI: 10.1016/S0021-9258(17)39445-0
关键词: Mitogen-activated protein kinase kinase 、 Myosin light-chain kinase 、 Myosin light chain kinase activity 、 Cyclin-dependent kinase 9 、 MAP kinase kinase kinase 、 Biochemistry 、 Cyclin-dependent kinase 2 、 Chemistry 、 MAP2K7 、 P70-S6 Kinase 1 、 Cell biology 、 Molecular biology
摘要: Smooth muscle myosin light chain kinase is phosphorylated in vitro by protein C purified from human platelets. When which has calmodulin bound C, 0.8-1.1 mol of phosphate incorporated per with no effect on its enzyme activity. Phosphorylation results the incorporation 2-2.4 and significantly decreases rate The decrease activity due to a 3.3-fold increase concentration necessary for half-maximal activation kinase. sites catalytic subunit cAMP-dependent were compared two-dimensional peptide mapping following extensive tryptic digestion single site when (site 3) different that 1). additional not appears be same 2). These studies confirm important role 2 binding Sequential using both suggest phosphorylation 1 also plays part decreasing affinity calmodulin.
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