Protein kinase C and cAMP‐dependent protein kinase induce opposite effects on actin polymerizability

FEBS Letters

Nishida, Eisuke²  Akiyama, Tetsu¹  Sakai, Hikoichi²  Ohta, Yasutaka² 

[1] Department of Pathology, Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606, Japan;>Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Hongo, Tokyo 113 Japan

关键词: Protein kinase C;    Actin;    cyclic AMP-dependent protein kinase;    Cytoskeleton;    Signal transduction;   

DOI  :  10.1016/0014-5793(87)80391-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Protein kinase C phosphorylated muscle and non-muscle monomeric actin more efficiently than filamentous actin in vitro. By sedimentation assay, the ratio of phosphorylated to unphosphorylated actin was much higher in sedimentable actin than in the non-sedimentable form, suggesting that phosphorylated actin was more readily incorporated into F-actin than unphosphorylated actin. In contrast, actin phosphorylated by cAMP-dependent protein kinase was found to have weaker polymerizability than the unphosphorylated form. The phosphopeptide mapping pattern of actin phosphorylated by protein kinase C was different from that of actin phosphorylated by cAMP-dependent protein kinase. Thus, both the protein kinases phosphorylate actin differently and induce opposite effects on actin polymerizability.

【 授权许可】

Unknown