Modifications of p53: competing for the lysines

被引：53

作者：

Carter, Stephanie ^{[1
]}

Vousden, Karen H. ^{[1
]}

机构：

[1] Beatson Inst Canc Res, Glasgow G61 1BD, Lanark, Scotland

来源：

CURRENT OPINION IN GENETICS & DEVELOPMENT | 2009年 / 19卷 / 01期

关键词：

UBIQUITIN LIGASE ACTIVITY; POSTTRANSLATIONAL MODIFICATIONS; NUCLEAR EXPORT; ACTIVATES P53; ACETYLATION; MDM2; NEDDYLATION; METHYLATION; SENESCENCE; DOMAIN;

D O I：

10.1016/j.gde.2008.11.010

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The p53 tumour suppressor protein is subject to numerous post-translational modifications, which coalesce in various combinations and patterns to regulate its activity. In addition to a multitude of phosphorylated serines and threonines, many of the lysine residues in p53 can be modified to regulate activity, stability and subcellular localization of the protein. This complexity is amplified by the variety of modifications that can target the same lysine residue - often with opposing effects on p53 function.

引用

页码：18 / 24

页数：7

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