Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

Xu Luo, Imawati Budihardjo, Hua Zou, Clive A. Slaughter, Xiaodong Wang

Research output: Contribution to journalArticle

2840 Citations (Scopus)

Abstract

We report here the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as Fas and TNF. Peptide mass fingerprinting identified this protein as Bid, a BH3 domain- containing protein known to interact with both Bcl2 and Bax. Caspase-8 cleaves Bid, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Immunodepletion of Bid from cell extracts eliminated the cytochrome c releasing activity. The cytochrome c releasing activity of Bid was antagonized by Bcl2. A mutation at the BH3 domain diminished its cytochrome c releasing activity. Bid, therefore, relays an apoptotic signal from the cell surface to mitochondria.

Original languageEnglish (US)
Pages (from-to)481-490
Number of pages10
JournalCell
Volume94
Issue number4
DOIs
StatePublished - Aug 21 1998
Externally publishedYes

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Death Domain Receptors
Mitochondria
Cell Surface Receptors
Cytochromes c
Cell Death
Chemical activation
Caspase 8
Proteins
BH3 Interacting Domain Death Agonist Protein
Peptide Mapping
Caspases
Cell Extracts
Purification
Peptides
Mutation

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. / Luo, Xu; Budihardjo, Imawati; Zou, Hua; Slaughter, Clive A.; Wang, Xiaodong.

In: Cell, Vol. 94, No. 4, 21.08.1998, p. 481-490.

Research output: Contribution to journalArticle

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