Protein kinase C and cAMP‐dependent protein kinase induce opposite effects on actin polymerizability
Authors:
- 5 October 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 222 (2) , 305-310
Abstract
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.Keywords
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