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

FEBS Lett. 1987 Oct 5;222(2):305-10. doi: 10.1016/0014-5793(87)80391-5.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism*
  • Animals
  • Binding Sites
  • Catalysis
  • Electrophoresis / methods
  • Muscles / metabolism
  • Phosphorylation
  • Polymers
  • Protein Kinase C / metabolism*
  • Protein Kinases / metabolism*
  • Rabbits
  • Rats


  • Actins
  • Polymers
  • Protein Kinases
  • Protein Kinase C