Brush border myosin heavy chain phosphorylation is regulated by calcium and calmodulin

FEBS Letters

Montibeller, Judith¹  Rieker, James P.¹  Swanljung-Collins, Helena¹  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 membrane;    Myosin;    Myosin heavy chain kinase;    Myosin light chain kinase;    Calmodulin;    (Chicken intestine);    CaM;    calmodulin;    PMSF;    phenylmethylsulfonyl fluoride;    DTT;    dithiothreitol;    PAGE;    polyacrylamide gel electrophoresis;    DATD;    N;    N '-diallyltartardiamide;    FPLC;    fast protein liquid chromatography;    LC20;    myosin 20 kDa light chain;   

DOI  :  10.1016/0014-5793(87)81576-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Myosin from chicken intestinal brush borders is phosphorylated on its heavy chains at threonine by a kinase isolated from brush borders. In contrast to other heavy chain kinases, the brush border kinase activity is dependent on calcium and calmodulin. The partially purified preparation also phosphorylated myosin on its light chains at serine, but in a calmodulin-independent manner. Phosphorylation of the light chains in the absence of calmodulin or both heavy and light chains in the presence of calmodulin activated its actinactivated ATPase activity about 10-fold, to about 50 per mg.

【 授权许可】

Unknown