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Protein kinase C and cAMP‐dependent protein kinase induce opposite effects on actin polymerizability
Author(s) -
Ohta Yasutaka,
Akiyama Tetsu,
Nishida Eisuke,
Sakai Hikoichi
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80391-5
Subject(s) - actin , protein kinase a , phosphorylation , actin binding protein , microbiology and biotechnology , kinase , actin remodeling , cyclin dependent kinase 2 , biology , protein phosphorylation , biochemistry , chemistry , actin cytoskeleton , cytoskeleton , cell
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.