Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4.
The two genes CED-4 and CED-3 (the nematode homologue of interleukin-1beta converting enzyme, ICE) of Caenorhabditis elegans are implicated in the control of cell death, but the mechanism by which this occurs is unknown. Here we provide evidence that CED-3 and CED-4 both contain sequences with homology to a domain present in RAIDD and the prodomain of certain ICE-like proteases (caspases). This domain is known to establish an interaction between RAIDD and these caspases. Similarly, CED-4 was found to interact with CED-3. Thus, the activity of the death protease CED-3 appears to be controlled by CED-4 through a direct physical interaction.
Irmler
M
M
Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland.
Hofmann
K
K
Vaux
D
D
Tschopp
J
J
D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000737:chemistry*; D029742:Caenorhabditis elegans Proteins; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D020169:Caspases; D015801:Helminth Proteins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D029742:Caenorhabditis elegans Proteins; D002135:Calcium-Binding Proteins; C089224:Ced-4 protein, C elegans; D015801:Helminth Proteins; D020169:Caspases; C089223:ced-3 protein, C elegans