Cancers 2015, 7(1), 30-69; doi:10.3390/cancers7010030
p53 Acetylation: Regulation and Consequences
1
Department of Pharmacology, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA
2
Medical Scientist Training Program, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA
3
Department of Pathology, The University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Rebecca S. Hartley
Received: 18 March 2014 / Accepted: 12 December 2014 / Published: 23 December 2014
(This article belongs to the Special Issue Cell Cycle Deregulation in Cancers)
Abstract
Post-translational modifications of p53 are critical in modulating its tumor suppressive functions. Ubiquitylation, for example, plays a major role in dictating p53 stability, subcellular localization and transcriptional vs. non-transcriptional activities. Less is known about p53 acetylation. It has been shown to govern p53 transcriptional activity, selection of growth inhibitory vs. apoptotic gene targets, and biological outcomes in response to diverse cellular insults. Yet recent in vivo evidence from mouse models questions the importance of p53 acetylation (at least at certain sites) as well as canonical p53 functions (cell cycle arrest, senescence and apoptosis) to tumor suppression. This review discusses the cumulative findings regarding p53 acetylation, with a focus on the acetyltransferases that modify p53 and the mechanisms regulating their activity. We also evaluate what is known regarding the influence of other post-translational modifications of p53 on its acetylation, and conclude with the current outlook on how p53 acetylation affects tumor suppression. Due to redundancies in p53 control and growing understanding that individual modifications largely fine-tune p53 activity rather than switch it on or off, many questions still remain about the physiological importance of p53 acetylation to its role in preventing cancer. View Full-TextKeywords:
p53; acetylation; post-translational modifications; transcription; histone acetyltransferases (HATs); p300/CBP; PCAF; MYST family HATs (Tip60; MOF; MOZ); tumor suppression
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
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MDPI and ACS Style
Reed, S.M.; Quelle, D.E. p53 Acetylation: Regulation and Consequences. Cancers 2015, 7, 30-69.