p53 regulation by ubiquitin

被引:165
作者
Brooks, Christopher L. [1 ]
Gu, Wei [2 ,3 ]
机构
[1] Stemline Therapeut Inc, New York, NY 10128 USA
[2] Columbia Univ, Coll Phys & Surg, Inst Canc Genet, New York, NY 10032 USA
[3] Columbia Univ, Coll Phys & Surg, Dept Pathol, New York, NY 10032 USA
关键词
p53; Mdm2; Antirepression; Destabilization; Ubiquitination; Transcriptional activation and stability; SMALL-MOLECULE INHIBITOR; DNA-BINDING DOMAIN; IN-VIVO; TRANSCRIPTIONAL ACTIVITY; TUMOR-SUPPRESSOR; LIGASE ACTIVITY; EMBRYONIC LETHALITY; NUCLEAR EXPORT; ACTIVATES P53; MOUSE MODELS;
D O I
10.1016/j.febslet.2011.05.022
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ubiquitination pathway is a highly dynamic and coordinated process that regulates degradation as well as numerous processes of proteins within a cell. The p53 tumor suppressor and several factors in the pathway are regulated by ubiquitin as well as ubiquitin-like proteins. These modifications are critical for the function of p53 and control both the degradation of the protein as well as localization and activity. Importantly, more recent studies have identified deubiquitination enzymes that can specifically remove ubiquitin moieties from p53 or other factors in the pathway, and the reversible nature of this process adds yet another layer of regulatory control of p53. This review highlights the recent advances in our knowledge of ubiquitin and the p53 pathway. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2803 / 2809
页数:7
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