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

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

Cell (1998-09-04)
X Luo, I Budihardjo, H Zou, C Slaughter, X Wang
RÉSUMÉ

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.

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Sigma-Aldrich
BID, Caspase-8-cleaved from mouse, ≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution
Sigma-Aldrich
BID human, ≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution