The Caenorhabditis elegans CED-9 protein does not directly inhibit the caspase CED-3, in vitro nor in yeast
- Author(s)
- Jabbour, AM; Ho, PK; Puryer, MA; Ashley, DM; Ekert, PG; Hawkins, CJ;
- Details
- Publication Year 2004-12,Volume 11,Issue #12,Page 1309-1316
- Journal Title
- CELL DEATH AND DIFFERENTIATION
- Publication Type
- Journal Article
- Abstract
- A genetically defined pathway orchestrates the removal of 131 of the 1090 somatic cells generated during the development of the hermaphrodite nematode Caenorhabditis elegans. Regulation of apoptosis is highly evolutionarily conserved and the nematode cell death pathway is a valuable model for studying mammalian apoptotic pathways, the dysregulation of which can contribute to numerous diseases. The nematode caspase CED-3 is ultimately responsible for the destruction of worm cells in response to apoptotic signals, but it must first be activated by CED-4. CED-9 inhibits programmed cell death and considerable data have demonstrated that CED-9 can directly bind and inhibit CED-4. However, it has been suggested that CED-9 may also directly inhibit CED-3. In this study, we used a yeast-based system and biochemical approaches to explore this second potential mechanism of action. While we confirmed the ability of CED-9 to inhibit CED-4, our data argue that CED-9 can not directly inhibit CED-3.
- Publisher
- NATURE PUBLISHING GROUP
- Keywords
- PROGRAMMED CELL-DEATH; C-ELEGANS; SACCHAROMYCES-CEREVISIAE; APOPTOSIS; REGULATORS; ACTIVATION; BCL-2; PREVENTION; ENCODES
- Publisher's Version
- https://doi.org/10.1038/sj.cdd.4401501
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2004-12-01 12:00:00