ATPase activity of the microvillar 110 kDa polypeptide‐calmodulin complex is activated in Mg2+ and inhibited in K+‐EDTA by F‐actin

FEBS Letters

Krizek, Janet¹  Bretscher, Anthony¹  Coluccio, Lynne M.¹ 

[1] Section of Biochemistry, Molecular and Cell Biology, Wing Hall, Cornell University, Ithaca, NY 14853, USA

关键词: Calmodulin;    Myosin;    Actin;    Microvillus;    Cytoskeleton;    ATPase;   

DOI  :  10.1016/0014-5793(87)81172-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Highly purified microvillar 110 kDa polypeptide-calmodulin (110 K-cam) complex was confirmed to have ATPase activities characteristic of a myosin. The effect of F-actin on these activities was investigated. The Mg²⁺-ATPase is activated about 2-fold by F-actin in a dose-dependent fashion, whereas the K⁺-EDTA -ATPase is inhibited by > 90% by F-actin. These data provide evidence for a functional relationship between the ATPase activity of 110K-cam and its interaction with F-actin. They also extend the similarities between 110K-cam and myosin. The results suggest that higher cells contain in addition to myosin a second class of myosin-like molecules represented by 110K-cam.

【 授权许可】

Unknown