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

Honglin Li, Hong Zhu, Chi Jie Xu, Junying Yuan

Research output: Contribution to journalArticle

3583 Scopus citations

Abstract

We report here that BID, a BH3 domain-containing proapoptotic Bc12 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.

Original languageEnglish (US)
Pages (from-to)491-501
Number of pages11
JournalCell
Volume94
Issue number4
DOIs
StatePublished - Aug 21 1998
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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