Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

被引：3815

作者：

Li, HL ^{[1
]}

Zhu, H ^{[1
]}

Xu, CJ ^{[1
]}

Yuan, JY ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Cell Biol, Boston, MA 02115 USA

来源：

CELL | 1998年 / 94卷 / 04期

关键词：

D O I：

10.1016/S0092-8674(00)81590-1

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：

We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria, tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion. Coexpression of Bclx(L) inhibits all the apoptotic changes induced by tBID. Our results indicate that BID is a mediator of mitochondrial damage induced by Casp8.

引用

页码：491 / 501

页数：11

共 43 条

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