Phosphorylation of brush border myosin by brush border calmodulin‐dependent myosin heavy and light chain kinases

FEBS Letters

Rieker, James P.¹  Collins, Jimmy H.¹ 

[1] Department of Microbiology, Biochemistry and Molecular Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA

关键词: Brush border myosin;    Myosin heavy chain kinase;    Myosin light chain kinase;    Calmodulin;    (Chicken);    CaM;    calmodulin;    PMSF;    phenylmethylsulfonyl fluoride;    DTT;    dithiothreitol;    PAGE;    polyacrylamide gel electrophoresis;    LC20;    myosin 20 kDa light chain;   

DOI  :  10.1016/0014-5793(87)80301-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Calmodulin-dependent myosin light chain kinase isolated from chicken intestinal brush border phosphorylates brush border myosin at an apparently single serine identical to that phosphorylated by smooth muscle myosin light chain kinase. Phosphorylation to 1.8 mol phosphate/mol myosin activated the myosin actin-activated ATPase about 10-fold, to about 50 nmol/min per mg. Myosin phosphorylated on its light chains could then be further phosphorylated to a total of 3.2 mol phosphate per mol by brush border calmodulin-dependent heavy chain kinase. Heavy chain phosphorylation did not alter the actin-activated ATPase of either myosin prephosphorylated on its light chains or of unphosphorylated myosin.

【 授权许可】

Unknown