Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm

Biochem J. 2003 Mar 1;370(Pt 2):361-71. doi: 10.1042/BJ20021626.

Abstract

Phosphorylation plays a central role in regulating the activation and signalling lifetime of protein kinases A, B (also known as Akt) and C. These kinases share three conserved phosphorylation motifs: the activation loop segment, the turn motif and the hydrophobic motif. This review focuses on how phosphorylation at each of these sites regulates the maturation, signalling and down-regulation of PKC as a paradigm for how these sites control the function of the ABC kinases.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • 3-Phosphoinositide-Dependent Protein Kinases
  • Amino Acid Motifs
  • Animals
  • Enzyme Activation
  • HSP70 Heat-Shock Proteins / metabolism
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism
  • Phosphorylation
  • Protein Kinase C / chemistry
  • Protein Kinase C / metabolism*
  • Protein Processing, Post-Translational / physiology
  • Protein-Serine-Threonine Kinases / metabolism

Substances

  • HSP70 Heat-Shock Proteins
  • Isoenzymes
  • 3-Phosphoinositide-Dependent Protein Kinases
  • Protein-Serine-Threonine Kinases
  • Protein Kinase C