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Protein & Cell

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ISSN 1674-8018(Online)

CN 11-5886/Q

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Prot Cell    2011, Vol. 2 Issue (6) : 456-462    https://doi.org/10.1007/s13238-011-1063-9      PMID: 21748595
MINI-REVIEW
The impact of acetylation and deacetylation on the p53 pathway
Christopher L. Brooks1(), Wei Gu2
1. Stemline Therapeutics, Inc., New York, NY 10128, USA; 2. Institute for Cancer Genetics, and Department of Pathology College of Physicians & Surgeons, Columbia University, New York, NY 10032, USA
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Abstract

The p53 tumor suppressor is a sequence-specific transcription factor that undergoes an abundance of post-translational modifications for its regulation and activation. Acetylation of p53 is an important reversible enzymatic process that occurs in response to DNA damage and genotoxic stress and is indispensible for p53 transcriptional activity. p53 was the first non-histone protein shown to be acetylated by histone acetyl transferases, and a number of more recent in vivo models have underscored the importance of this type of modification for p53 activity. Here, we review the current knowledge and recent findings of p53 acetylation and deacetylation and discuss the implications of these processes for the p53 pathway.
Keywords p53      Mdm2      acetylation      deacetylation      destabilization      ubiquitination      transcriptional activation and stability     
Corresponding Author(s): Brooks Christopher L.,Email:cbrooks@stemline.com   
Issue Date: 01 June 2011
 Cite this article:   
Christopher L. Brooks,Wei Gu. The impact of acetylation and deacetylation on the p53 pathway[J]. Prot Cell, 2011, 2(6): 456-462.
 URL:  
https://academic.hep.com.cn/pac/EN/10.1007/s13238-011-1063-9
https://academic.hep.com.cn/pac/EN/Y2011/V2/I6/456
Fig.1  Schematic diagram of p53 functional domains and overview of p53 acetylation sites.
The eight acetylation sites that are indispensible for p53 activation are indicated in red. The corresponding major modifying enzymes are also indicated.
Fig.1  Schematic diagram of p53 functional domains and overview of p53 acetylation sites.
The eight acetylation sites that are indispensible for p53 activation are indicated in red. The corresponding major modifying enzymes are also indicated.
Fig.2  The role of p53 acetylation in gene regulation.
(A) Unacetylated p53 is capable of activating genes that are involved in the negative regulation of p53, such as Mdm2, as a mechanism to keep p53 protein levels low during times of normal homeostasis. (B) Upon DNA damage, acetylation of p53 allows for the disruption of the Mdm2-p53 interaction and the recruitment of specific HATs to the promoters of genes involved in DNA repair and cell cycle control. (C) Full acetylation of p53 at all key acetylation sites promotes the activation of proapoptotic genes. (D) SIRT1 and HDAC1 are deacetylases that can reverse p53 acetylation and lead to transcriptional repression.
Fig.2  The role of p53 acetylation in gene regulation.
(A) Unacetylated p53 is capable of activating genes that are involved in the negative regulation of p53, such as Mdm2, as a mechanism to keep p53 protein levels low during times of normal homeostasis. (B) Upon DNA damage, acetylation of p53 allows for the disruption of the Mdm2-p53 interaction and the recruitment of specific HATs to the promoters of genes involved in DNA repair and cell cycle control. (C) Full acetylation of p53 at all key acetylation sites promotes the activation of proapoptotic genes. (D) SIRT1 and HDAC1 are deacetylases that can reverse p53 acetylation and lead to transcriptional repression.
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