Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis

被引：471

作者：

Zha, JP

Weiler, S

Oh, KJ

Wei, MC

Korsmeyer, SJ ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Pathol, Dana Farber Canc Inst,Howard Hughes Med Inst, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Dept Med, Dana Farber Canc Inst,Howard Hughes Med Inst, Boston, MA 02115 USA

来源：

SCIENCE | 2000年 / 290卷 / 5497期

关键词：

D O I：

10.1126/science.290.5497.1761

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Many apoptotic molecules relocate subcellularly in cells undergoing apoptosis. The pro-apoptotic protein BID underwent posttranslational (rather than classic cotranslational) N-myristoylation when cleavage by caspase 8 caused exposure of a glycine residue. N-myristoylation enabled the targeting of a complex of p7 and myristoylated p15 fragments of BID to artificial membranes bearing the Lipid composition of mitochondria, as well as to intact mitochondria. This post-proteolytic N-myristoylation serves as an activating switch, enhancing BID-induced release of cytochrome c and cell death.

引用

页码：1761 / 1765

页数：5

共 24 条

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