Apoptosomes: engines for caspase activation
- Details
- Publication Year 2002-12,Volume 14,Issue #6,Page 715-720
- Journal Title
- CURRENT OPINION IN CELL BIOLOGY
- Publication Type
- Journal Article
- Abstract
- Activation of the caspases that initiate apoptosis typically requires cognate scaffold proteins, including CED-4 in Caenorhabditis elegans, Apaf-1 in mammals and Dark in Drosophila. Each scaffold protein oligomerizes procaspases into a complex called the apoptosome, but the regulation and biological roles of the scaffolds differ. Whereas CED-4 is restrained by the Bcl-2 homologue CED-9, Apaf-1 is inhibited by its WD40 repeat region, until it is activated by cytochrome c, derived from damaged mitochondria. Although Dark also has a WD40 region, its activation does not seem to involve cytochrome c. CED-4 is essential for apoptosis in the worm and Dark for many apoptotic responses in the fly, but the Apaf-1/caspase-9 system probably amplifies rather than initiates the mammalian caspase cascade.
- Publisher
- CURRENT BIOLOGY LTD
- Keywords
- PROGRAMMED CELL-DEATH; BCL-2 FAMILY MEMBERS; CYTOCHROME-C; CAENORHABDITIS-ELEGANS; MEDIATED OLIGOMERIZATION; PROCASPASE-9 ACTIVATION; NEGATIVE REGULATION; DROSOPHILA HOMOLOG; APAF-1 APOPTOSOME; IN-VIVO
- Publisher's Version
- https://doi.org/10.1016/S0955-0674(02)00381-2
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2002-12-01 12:00:00