CED-4 forms a 2 : 2 heterotetrameric complex with CED-9 until specifically displaced by EGL-1 or CED-13
Publication Year 2006-03, Volume 13, Issue #3, Page 426-434
- Journal Title
- CELL DEATH AND DIFFERENTIATION
- Publication Type
- Journal Article
- The pathway to cell death in Caenorhabditis elegans is well established. In cells undergoing apoptosis, the Bcl-2 homology domain 3 (BH3)-only protein EGL-1 binds to CED-9 at the mitochondrial membrane to cause the release of CED-4, which oligomerises and facilitates the activation of the caspase CED-3. However, despite many studies, the biophysical features of the CED-4/CED-9 complex have not been fully characterised. Here, we report the purification of a soluble and stable 2 : 2 heterotetrameric complex formed by recombinant CED-4 and CED-9 coexpressed in bacteria. Consistent with previous studies, synthetic peptides corresponding to the BH3 domains of worm BH3-only proteins (EGL-1, CED-13) dissociate CED-4 from CED-9, but not from the gain-of-function CED-9 (G169E) mutant. Surprisingly, the ability of worm BH3 domains to dissociate CED-4 was specific since mammalian BH3-only proteins could not do so.
- NATURE PUBLISHING GROUP
- PROGRAMMED CELL-DEATH; CAENORHABDITIS-ELEGANS; PROTEIN CED-9; REGULATORS CED-9; BCL-2; ACTIVATION; APOPTOSIS; OLIGOMERIZATION; RECOGNITION; MECHANISM
- Publisher's Version
- Rights Notice
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Creation Date: 2006-03-01 12:00:00Last Modified: 0001-01-01 12:00:00