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. 2000 Nov 16;408(6810):377-81.
doi: 10.1038/35042612.

Deacetylation of p53 modulates its effect on cell growth and apoptosis

J Luo  1 , F Su, D Chen, A Shiloh, W Gu
Affiliations

Deacetylation of p53 modulates its effect on cell growth and apoptosis

J Luo et al. Nature. .

Abstract

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.

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