Journal
PROTEIN & CELL
Volume 2, Issue 6, Pages 456-462Publisher
HIGHER EDUCATION PRESS
DOI: 10.1007/s13238-011-1063-9
Keywords
p53; Mdm2; acetylation; deacetylation; destabilization; ubiquitination; transcriptional activation and stability
Categories
Funding
- NCI NIH HHS [R01 CA085533, R01 CA118561, R01 CA098821, P01 CA097403, R01 CA131439, R01 CA129627, P01 CA080058] Funding Source: Medline
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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.
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