Phosphorylation of brush border myosin at threonine on its 20 kDa light chains by a calmodulin‐independent kinase activates its ATPase

FEBS Letters

Montibeller, Judith¹  Rieker, James P.¹  Borysenko, Christopher¹  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: Myosin;    Myosin light chain kinase;    Myosin actin-activated ATPase;    Calmodulin;    Cell motility;    (Chicken intestinal brush border);   

DOI  :  10.1016/0014-5793(88)81252-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A calmodulin-independent kinase isolated from chicken intestinal brush border phosphorylates brush border myosin mainly at an apparently single threonine on its 20 kDa light chains. Phosphorylation to 1.9 mol phosphate/mol myosin activated the myosin actin-activated ATPase about 12-fold, to about 100 nmol/min per mg. Brush border myosin ATPase can thus be activated by phosphorylation either at threonine, by calmodulin-independent kinase, or at serine, by calmodulin-dependent myosin light chain kinase, as previously shown [(1987) FEBS Lett. 223, 262–266].

【 授权许可】

Unknown