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| Caspase-9, Bcl-X-L, and Apaf-1 form a ternary complex |
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| Author(s): Pan GH, O'Rourke K, Dixit VM |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 273 Issue: 10 Pages: 5841-5845 Published: MAR 6 1998 |
| Times Cited: 395 References: 31 |
| Abstract: Genetic analysis of apoptosis in the nematode Caenorhabditis elegans has revealed the cell death machine to be composed of three core interacting components. CED-4 (equivalent to mammalian Apaf-1) is a nucleotide binding molecule that complexes with the zymogen form of the death protease CED-3, leading to its autoactivation and cell death, CED-9 blocks death by complexing with CED-4 and attenuating its ability to promote CED-3 activation, An equivalent ternary complex was found to be present in mammalian cells involving Apaf-1, the mammalian death protease caspase-9, and Bcl-X-L, an anti-apoptotic member of the Bcl-2 family, Consistent with a central role for caspase-9, a dominant negative form effectively inhibited cell death initiated by a wide variety of inducers. |
| Document Type: Article |
| Language: English |
| Reprint Address: Dixit, VM (reprint author), Genentech Inc, 1 DNA Way,M-S-40, S San Francisco, CA 94080 USA |
Addresses:
1. Univ Michigan, Sch Med, Dept Pathol, Ann Arbor, MI 48109 USA |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: ZA256 |
| ISSN: 0021-9258 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |