Mature DIABLO/Smac is produced by the IMP protease complex on the mitochondrial inner membrane

被引：74

作者：

Burri, L

Strahm, Y

Hawkins, CJ

Gentle, IE

Puryer, MA

Verhagen, A

Callus, B

Vaux, D

Lithgow, T ^{[1
]}

机构：

[1] Univ Melbourne, Russell Grimwade Sch Biochem & Mol Biol, Parkville, Vic 3010, Australia

[2] Monash Univ, Victoriam Bioinformat Consortium, Clayton, Vic 3800, Australia

[3] Royal Childrens Hosp, Murdoch Childrens Res Inst, Childrens Canc Ctr, Parkville, Vic 3052, Australia

[4] Walter & Eliza Hall Inst Med Res, Parkville, Vic 3050, Australia

[5] Bio21 Mol Sci & Biotechnol Inst, Parkville, Vic 3010, Australia

来源：

MOLECULAR BIOLOGY OF THE CELL | 2005年 / 16卷 / 06期

关键词：

D O I：

10.1091/mbc.E04-12-1086

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

DIABLO/Smac is a mitochondrial protein that can promote apoptosis by promoting the release and activation of caspases. To do so, DIABLO/Smac must first be processed by a mitochondrial protease and then released into the cytosol, and we show this in an intact cellular system. We propose that the precursor form of DIABLO/Smac enters the mitochondria through a stop-transfer pathway and is processed to its active form by the inner membrane peptidase (IMP) complex. Catalytic subunits of the mammalian IMP complex were identified based on sequence conservation and functional complementation, and the novel sequence motif RX5P in Imp1 and NX5S in Imp2 distinguish the two catalytic subunits. DIABLO/Smac is one of only a few specific proteins identified as substrates for the IMP complex in the mitochondrial intermembrane space.

引用

页码：2926 / 2933

页数：8

共 58 条

[1] Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli [J].