Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4

FEBS Lett. 1997 Apr 7;406(1-2):189-90. doi: 10.1016/s0014-5793(97)00271-8.

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Caenorhabditis elegans / chemistry*
  • Caenorhabditis elegans Proteins*
  • Calcium-Binding Proteins / chemistry*
  • Caspases*
  • Helminth Proteins / chemistry*
  • Humans
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid

Substances

  • Caenorhabditis elegans Proteins
  • Calcium-Binding Proteins
  • Ced-4 protein, C elegans
  • Helminth Proteins
  • Caspases
  • ced-3 protein, C elegans