The Impact of Acetylation and Deacetylation on the p53 Pathway

Protein Cell. 2011 Jun;2(6):456-62. doi: 10.1007/s13238-011-1063-9. Epub 2011 Jul 12.

Abstract

The p53 tumor suppressor is a sequence-specific transcription factor that undergoes an abundance of post-translational modifications for its regulation and activation. Acetylation of p53 is an important reversible enzymatic process that occurs in response to DNA damage and genotoxic stress and is indispensible for p53 transcriptional activity. p53 was the first non-histone protein shown to be acetylated by histone acetyl transferases, and a number of more recent in vivo models have underscored the importance of this type of modification for p53 activity. Here, we review the current knowledge and recent findings of p53 acetylation and deacetylation and discuss the implications of these processes for the p53 pathway.

Publication types

  • Review

MeSH terms

  • Acetylation
  • Animals
  • DNA Damage
  • Gene Expression Regulation*
  • Histone Acetyltransferases / metabolism*
  • Humans
  • Mice
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary / genetics*
  • Signal Transduction / physiology*
  • Tumor Suppressor Protein p53* / genetics
  • Tumor Suppressor Protein p53* / metabolism
  • Ubiquitination

Substances

  • Tumor Suppressor Protein p53
  • Histone Acetyltransferases