Molecular and Cellular Biochemistry

, Volume 142, Issue 2, pp 125–130 | Cite as

Membrane components can modulate the substrate specificity of protein kinase C

  • Robert H. Bruins
  • Richard M. Epand
Article
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Accepted:

Abstract

The cationic amphiphile, cholesteryl-3β-carboxyamidoethylene-trimethylammonium iodide, can alter the substrate specificity of protein kinase C (PKC). The phosphorylation of histone catalyzed by PKC requires the binding of the enzyme to phospholipid vesicles. This cationic amphiphile reduces both the binding of PKC to lipid and as a consequence its rate of phosphorylation of histone. In contrast, PKC bound to large unilamellar vesicles (LUVs) composed of 50 mol % POPS, 20 mol % POPC, and 30 mol % of this amphiphile catalyzes protamine sulfate phosphorylation by an almost 4 fold greater rate. This activation requires phosphatidylserine (PS) and is inhibited by Ca2+. The extent of activation is affected by the time of incubation of PKC with LUVs. This data suggests a novel mechanism by which PKC-dependent signal transduction pathways may be altered by altering the protein targets of this enzyme.

Key Words

protein kinase C substrate specificity cationic amphiphiles 
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Copyright information

© Kluwer Academic Publishers 1995

Authors and Affiliations

  • Robert H. Bruins
    • 1
  • Richard M. Epand
    • 1
  1. 1.Department of BiochemistryMcMaster UniversityHamiltonCanada

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