The intricacies of p21 phosphorylation - Protein/protein interactions, subcellular localization and stability

被引：151

作者：

Child, Emma S. ^{[1
]}

Mann, David J. ^{[1
]}

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Fac Nat Sci, Div Cell & Mol Biol, London SW7 2AZ, England

来源：

CELL CYCLE | 2006年 / 5卷 / 12期

基金：

英国生物技术与生命科学研究理事会;

关键词：

Akt/PKB; p21; Cip1; Waf1; Sdi1; cyclin; cdk; cell cycle; phosphorylation; degradation; protein/protein interaction; PKC; p27; Kip1;

D O I：

10.4161/cc.5.12.2863

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

p21 was originally described as functioning as a cell cycle regulator via inhibition of both cyclin-dependent kinases and processive DNA replication. Nowadays it is recognized to play other fundamental roles including transcriptional regulation and the modulation of apoptosis. Each of these functions of p21 is achieved through direct p21/protein interactions and the subcellular localization of p21 plays an important part in dictating the binding partners to which p21 is exposed. Over recent years, a number of phosphorylation sites in p21 have been identified, these being targeted by several important intracellular signalling protein kinases. Here we review the state of our knowledge of p21 phosphorylation with respect to the kinases involved and the molecular biological effects of each phosphorylation event.

引用

页码：1313 / 1319

页数：7

共 104 条

[21] Glycogen synthase kinase 3β regulates cyclin D1 proteolysis and subcellular localization [J].