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The complexity of p53 stabilization and activation

Citation

Lavin, MF and Guven, N, The complexity of p53 stabilization and activation, Cell Death and Differentiation, 13, (6) pp. 941-950. ISSN 1350-9047 (2006) [Refereed Article]

DOI: doi:10.1038/sj.cdd.4401925

Abstract

A number of proteins are activated by stress stimuli but none so spectacularly or with the degree of complexity as the tumour suppressor p53 (human p53 gene or protein). Once stabilized, p53 is responsible for the transcriptional activation of a series of proteins involved in cell cycle control, apoptosis and senescence. This protein is present at low levels in resting cells but after exposure to DNA-damaging agents and other stress stimuli it is stabilized and activated by a series of post-translational modifications that free it from MDM2 (mouse double minute 2 but used interchangeably to denote human also), a ubiquination ligase that ubiquitinates it prior to proteasome degradation. The stability of p53 is also influenced by a series of other interacting proteins. In this review, we discuss the post-translational modifications to p53 in response to different stresses and the consequences of these changes.

Item Details

Item Type:Refereed Article
Keywords:p53, signal transduction, stabilisation
Research Division:Biological Sciences
Research Group:Biochemistry and Cell Biology
Research Field:Signal Transduction
Objective Division:Expanding Knowledge
Objective Group:Expanding Knowledge
Objective Field:Expanding Knowledge in the Biological Sciences
Author:Guven, N (Dr Nuri Guven)
ID Code:96208
Year Published:2006
Web of Science® Times Cited:411
Deposited By:Pharmacy
Deposited On:2014-10-24
Last Modified:2014-10-24
Downloads:0

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