| First Author | Luo X | Year | 1998 |
| Journal | Cell | Volume | 94 |
| Issue | 4 | Pages | 481-90 |
| PubMed ID | 9727491 | Mgi Jnum | J:49396 |
| Mgi Id | MGI:1277441 | Doi | 10.1016/s0092-8674(00)81589-5 |
| Citation | Luo X, et al. (1998) Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94(4):481-90 |
| abstractText | 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. |
