Deacetylation of p53 modulates its effect on cell growth and apoptosis

Jianyuan Luo, Fei Su, Delin Chen, Ariel Shiloh and Wei Gu
Additional contact information
Jianyuan Luo: College of Physicians & Surgeons, Columbia University
Fei Su: College of Physicians & Surgeons, Columbia University
Delin Chen: College of Physicians & Surgeons, Columbia University
Ariel Shiloh: College of Physicians & Surgeons, Columbia University
Wei Gu: College of Physicians & Surgeons, Columbia University

Nature, 2000, vol. 408, issue 6810, 377-381

Abstract: Abstract The p53 tumour suppressor is a transcriptional factor whose activity is modulated by protein stability and post-translational modifications including acetylation1,2,3,4. 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 complex5,6,7. 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.

Date: 2000
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/35042612 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:408:y:2000:i:6810:d:10.1038_35042612

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/35042612

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().