Identification of actin kinase activity in purified fragmin—actin complex

FEBS Letters

Hatano, Sadashi¹  Furuhashi, Kiyoshi¹ 

[1] Department of Molecular Biology, School of Science, Nagoya University, Chikusa-ku, Nagoya 464-01, Japan

关键词: Cytoskeleton;    Actin filament;    Phosphorylation;    Actin regulatory protein;   

DOI  :  10.1016/0014-5793(92)81140-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Actin kinase phosphorylates actin of fragmin—actin complex, resulting in the inactivation of the nucleation and capping activities of the complex. Fragmin—actin complex was prepared by a new purification procedure. Incubation with ATP caused inactivation of the purified complex and phosphorylation of actin of fragmin—actin complex. The detailed analysis of the complex by SDS-gel electrophoresis showed that actin kinase was co-purified with the fragmin—actin complex. Formation of such an association between actin kinase and substrate suggests that the kinase is localized on the fragmin—actin complex to efficiently regulate actin cytoskeletons.

【 授权许可】

Unknown