Abstract
P53 is one of the most important tumour suppressor proteins. While its activity seems to be dispensable for normal proliferating cells, this protein is required to maintain genomic integrity after DNA damage. In response to cellular stress, the amount of p53 protein accumulates and fulfils its function as a transcription factor. Most of the genes that are regulated by p53 control progression through the cell cycle or initiate cell death. A large number of proteins have been identified in recent years that control the activity of this important tumour suppressor protein. These proteins regulate the turnover of p53, its association with co-repressor and co-activator proteins and target gene promoters or impinge on p53 oligomerisation. This review shall give an overview of our current knowledge on how the activity of the p53 protein is controlled.
Keywords: p53, DNA damage, phosphorylation, acetylation, ubiquitination, protein-protein interactions
Current Chemical Biology
Title: Regulation of p53 Activity
Volume: 4 Issue: 1
Author(s): Karen A. Boehme and Christine Blattner
Affiliation:
Keywords: p53, DNA damage, phosphorylation, acetylation, ubiquitination, protein-protein interactions
Abstract: P53 is one of the most important tumour suppressor proteins. While its activity seems to be dispensable for normal proliferating cells, this protein is required to maintain genomic integrity after DNA damage. In response to cellular stress, the amount of p53 protein accumulates and fulfils its function as a transcription factor. Most of the genes that are regulated by p53 control progression through the cell cycle or initiate cell death. A large number of proteins have been identified in recent years that control the activity of this important tumour suppressor protein. These proteins regulate the turnover of p53, its association with co-repressor and co-activator proteins and target gene promoters or impinge on p53 oligomerisation. This review shall give an overview of our current knowledge on how the activity of the p53 protein is controlled.
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Cite this article as:
Boehme A. Karen and Blattner Christine, Regulation of p53 Activity, Current Chemical Biology 2010; 4 (1) . https://dx.doi.org/10.2174/2212796811004010001
DOI https://dx.doi.org/10.2174/2212796811004010001 |
Print ISSN 2212-7968 |
Publisher Name Bentham Science Publisher |
Online ISSN 1872-3136 |
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