Serine/threonine protein phosphatases PP1 and PP2A are key players in apoptosis

被引：146

作者：

Garcia, A

Cayla, X

Guergnon, J

Dessauge, F

Hospital, V

Rebollo, MP

Fleischer, A

Rebollo, A

机构：

[1] Inst Pasteur, Dept Parasitol, URA CNRS 2581, Lab Signalisat Immunoparasitaire, F-75015 Paris, France

[2] Univ Tours, UMR 6073 INRA CNRS, F-37380 Nouzilly, France

[3] Hosp Gen Leon, Leon, Spain

[4] Hop La Pitie Salpetriere, INSERM U543, Lab Immunol Cellulaire & Tissulaire, F-75013 Paris, France

来源：

BIOCHIMIE | 2003年 / 85卷 / 08期

关键词：

apoptosis; PP1; PP2A; Bcl-2; bad;

D O I：

10.1016/j.biochi.2003.09.004

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 reversible phosphorylation of proteins controlled by protein kinases and protein phosphatases is a major mechanism that regulates a wide variety of cellular processes. In contrast to C elegans, recent studies in mammalian cells have highlighted a major role of serine/threonine protein phosphorylation in apoptosis. To illustrate the importance of dephosphorylation processes in apoptosis, this review will focus on recent studies suggesting that the interaction of the serine/threonine protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) with certain regulators of the Bcl-2 family is critically involved in the control of apoptosis. (C) 2003 Editions scientifiques et medicales Elsevier SAS. All rights reserved.

引用

页码：721 / 726

页数：6

共 52 条

[41] Phosphorylation of Bcl2 and regulation of apoptosis [J].