Deacetylation of p53 modulates its effect on cell growth and apoptosis.

The p53 tumour suppressor is a transcriptional factor whose activity is modulated by protein stability and post-translational modifications including acetylation. The mechanism by which acetylated p53 is maintained in vivo remains unclear. Here we show that the deacetylation of p53 is mediated by an histone deacetylase-1 (HDAC1)-containing complex. We have ...
also purified a p53 target protein in the deacetylase complexes (designated PID; but identical to metastasis-associated protein 2 (MTA2)), which has been identified as a component of the NuRD complex. PID specifically interacts with p53 both in vitro and in vivo, and its expression reduces significantly the steady-state levels of acetylated p53. PID expression strongly represses p53-dependent transcriptional activation, and, notably, it modulates p53-mediated cell growth arrest and apoptosis. These results show that deacetylation and functional interactions by the PID/MTA2-associated NuRD complex may represent an important pathway to regulate p53 function.
Mesh Terms:
Acetylation, Amino Acid Sequence, Animals, Apoptosis, Carrier Proteins, Cell Division, Cell Line, Glutathione Transferase, Hela Cells, Histone Deacetylase 1, Histone Deacetylases, Humans, Mi-2 Nucleosome Remodeling and Deacetylase Complex, Mice, Molecular Sequence Data, Protein Binding, Proteins, Recombinant Fusion Proteins, Repressor Proteins, Sin3 Histone Deacetylase and Corepressor Complex, Transcriptional Activation, Tumor Suppressor Protein p53
Nature
Date: Nov. 16, 2000
Download Curated Data For This Publication
113187
Switch View:
  • Interactions 4