Phosphorylation by protein kinase CK2:: A signaling switch for the caspase-inhibiting protein ARC

被引：140

作者：

Li, PF

Li, JC

Müller, EC

Otto, A

Dietz, R

von Harsdorf, R ^{[1
]}

机构：

[1] Max Delbruck Ctr Mol Med, D-13125 Berlin, Germany

[2] Humboldt Univ, Charite, Dept Cardiol, D-13353 Berlin, Germany

来源：

MOLECULAR CELL | 2002年 / 10卷 / 02期

关键词：

D O I：

10.1016/S1097-2765(02)00600-7

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：

Caspases play a central role in apoptosis, but their activity is under the control of caspase-inhibiting proteins. A characteristic of caspase-inhibiting proteins is direct caspase binding. It is yet unknown how the localization of caspase-inhibiting proteins is regulated and whether there are upstream signals controlling their function. Here we report that the function of ARC is regulated by protein kinase CK2. ARC at threonine 149 is phosphorylated by CK2. This phosphorylation targets ARC to mitochondria. ARC is able to bind to caspase-8 only when it is localized to mitochondria but not to the cytoplasm. Our results reveal a molecular mechanism by which a caspase-inhibiting protein requires phosphorylation in order to prevent apoptosis.

引用

页码：247 / 258

页数：12

共 54 条

[21] Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3 [J].