Deacetylation of p53 modulates its effect on cell growth and apoptosis View Full Text


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Article Info

DATE

2000-11

AUTHORS

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

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. More... »

PAGES

377

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/35042612

DOI

http://dx.doi.org/10.1038/35042612

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019085837

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11099047


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