Cell. 1998 Aug 21;94(4):481-90.

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

Luo X, Budihardjo I, Zou H, Slaughter C, Wang X.

Source

Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, 75235, USA.

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.

PMID:: 9727491; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

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Grant Support

R01GM-57158/GM/NIGMS NIH HHS/United States

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Research Materials

anti-BH3 Interacting Domain Death Agonist (BID) antibody - antibodies-online

Miscellaneous

Mouse Genome Informatics (MGI)

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Related citations in PubMed

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. [Cell. 1998]
Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.
Li H, Zhu H, Xu CJ, Yuan J. Cell. 1998 Aug 21; 94(4):491-501.
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Cell. 1998 Aug 21 ;94(4):481-90.

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