Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy

被引：40

作者：

Allende-Vega, Nerea ^{[1
]}

Saville, Mark K. ^{[1
]}

机构：

[1] Univ Dundee, Ninewells Hosp & Med Sch, Dept Surg & Mol Oncol, CR UK Cell Transformat Res Grp, Dundee DD1 9SY, Scotland

来源：

SEMINARS IN CANCER BIOLOGY | 2010年 / 20卷 / 01期

关键词：

Ubiquitin; P53; Mdm2; MdmX; 26S proteasome; E1; E2; E3; Deubiquitinating enzyme; SMALL-MOLECULE INHIBITORS; EARLY EMBRYONIC LETHALITY; TUMOR-SUPPRESSOR PROTEIN; CELL-CYCLE ARREST; IN-VIVO; DNA-DAMAGE; LIGASE ACTIVITY; PROSTATE-CANCER; MDM2; PROMOTES; COLON-CANCER;

D O I：

10.1016/j.semcancer.2009.10.004

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 [肿瘤学];

摘要：

Ubiquitination plays a key role in regulating the tumour suppressor p53. It targets p53 for degradation by the 26S proteasome. The ubiquitin pathway also regulates the activity and localisation of p53. Ubiquitination requires ubiquitin-activating and -conjugating enzymes and ubiquitin ligases. In addition, ubiquitination can be reversed by the action of deubiquitinating enzymes. Here we give an overview of the role of components of the ubiquitin-proteasome system in the regulation of p53 and review progress in targeting these proteins to activate wild-type p53 for the treatment of cancer. (C) 2009 Published by Elsevier Ltd.

引用

页码：29 / 39

页数：11

共 194 条

[1]

ALLENDEVEGA N, 2009, ONCOGENE IN PRESS

[2]

Amerik AY, 1997, EMBO J, V16, P4826

[3]

Mdm2 and Mdm4 loss regulates distinct p53 activities [J].