p53 ubiquitination: Mdm2 and beyond

被引：704

作者：

Brooks, CL

Gu, W

机构：

[1] Columbia Univ, Coll Phys & Surg, Inst Canc Genet, New York, NY 10032 USA

[2] Columbia Univ, Coll Phys & Surg, Dept Pathol, New York, NY 10032 USA

来源：

MOLECULAR CELL | 2006年 / 21卷 / 03期

关键词：

D O I：

10.1016/j.molcel.2006.01.020

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：

Although early studies have suggested that the oncoprotein Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. The discoveries of MdmX, HAUSP, ARF, COP1, Pirh2, and ARF-BP1 continue to uncover the multiple facets of this pathway. There is no question that Mdm2 plays a pivotal role in downregulating p53 activities in numerous cellular settings. Nevertheless, growing evidence challenges the conventional view that Mdm2 is essential for p53 turnover.

引用

页码：307 / 315

页数：9

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