Phosphorylation of PPARs: from molecular characterization to physiological relevance

Biochimie. 2005 Jan;87(1):33-8. doi: 10.1016/j.biochi.2004.11.010.

Abstract

In addition to their ligand-mediated activation, nuclear receptor activity is finely tuned by their phosphorylation status. PPARs are phosphorylated by several kinases (PKA, PKC, MAPKs, and AMPK), which affect their activity in a ligand-dependent or -independent manner according to the isoform and cellular context. Molecular consequences are multiple, including changes in ligand affinity, DNA binding, recruitment of transcriptional cofactors, proteasome degradation... Finally, the physiological relevance of PPAR phosphorylation is discussed.

Publication types

  • Review

MeSH terms

  • AMP-Activated Protein Kinases
  • Animals
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Humans
  • Mitogen-Activated Protein Kinases / metabolism
  • Multienzyme Complexes / metabolism
  • PPAR alpha / metabolism
  • PPAR delta / metabolism
  • PPAR gamma / metabolism
  • Peroxisome Proliferator-Activated Receptors / metabolism*
  • Phosphorylation
  • Protein Kinase C / metabolism
  • Protein-Serine-Threonine Kinases / metabolism

Substances

  • Multienzyme Complexes
  • PPAR alpha
  • PPAR delta
  • PPAR gamma
  • Peroxisome Proliferator-Activated Receptors
  • Protein-Serine-Threonine Kinases
  • Cyclic AMP-Dependent Protein Kinases
  • Protein Kinase C
  • Mitogen-Activated Protein Kinases
  • AMP-Activated Protein Kinases