Next Article in Journal
Intertwining of Activin A and TGFβ Signaling: Dual Roles in Cancer Progression and Cancer Cell Invasion
Previous Article in Journal
Regulation of the Tumor-Suppressor Function of the Class III Phosphatidylinositol 3-Kinase Complex by Ubiquitin and SUMO
Previous Article in Special Issue
Situational Awareness: Regulation of the Myb Transcription Factor in Differentiation, the Cell Cycle and Oncogenesis
Article Menu

Export Article

Open AccessReview
Cancers 2015, 7(1), 30-69; doi:10.3390/cancers7010030

p53 Acetylation: Regulation and Consequences

1,2
and
1,2,3,*
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)
View Full-Text   |   Download PDF [1218 KB, uploaded 23 December 2014]   |  

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-Text
Keywords: p53; acetylation; post-translational modifications; transcription; histone acetyltransferases (HATs); p300/CBP; PCAF; MYST family HATs (Tip60; MOF; MOZ); tumor suppression p53; acetylation; post-translational modifications; transcription; histone acetyltransferases (HATs); p300/CBP; PCAF; MYST family HATs (Tip60; MOF; MOZ); tumor suppression
Figures

Figure 1

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).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Reed, S.M.; Quelle, D.E. p53 Acetylation: Regulation and Consequences. Cancers 2015, 7, 30-69.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Cancers EISSN 2072-6694 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top