Death Effector Domain (DED) found in DEDD2. DEDD2 has been shown to bind to itself, DEDD, and to the two tandem DED-containing caspases, caspase-8 and -10. It may play a role in apoptosis. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways.
Comment:The charge triad is part of a signature motif (E/D-RxDL) that is present in the DED family but not in other families of death domains (DD, CARD or Pyrin).
Comment:The charge triad is essential for the function of some DED-containing proteins. In FLIP, it is involved in the interaction with FADD to block apoptosis. In PEA15, the triad is necessary for interaction with ERK MAP kinase.