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 Slaughter, Xiaodong Wang

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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

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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