The apoptotic signal coming from ligand-induced oligomerization of death
receptors is mediated by a number of adaptor proteins containing specialized
interaction domains. Besides the death effector domain (DED), this group is
formed by the death domain (DD) (see <PDOC50017>) and the caspase recruitment
domain (CARD) (see <PDOC50209>).
The death effector domain was first described in the FADD/Mort1 protein 
and later shown to also occur in several other proteins [2,3]. The DED
typically associates with other DED-containing proteins, forming either dimers
or trimers [2,3,4]. It has been predicted that the DED is related in structure
and sequence to both DD and CARD domains, which work in similar pathways and
show similar interaction properties . Important members of the DED family
FADD/MORT1 death adaptor protein.
Caspase-8 (EC 3.4.22.-), upstream death protease, interacts with FADD.
Caspase-10 (EC 3.4.22.-).
v-FLIP, FLICE(caspase)-inhibitors that occur in γ herpesviruses and the
poxvirus MCV, interact with FADD and/or Caspase-8.
c-FLIP, cellular FLICE-inhibitor with inactive caspase domain, interacts
with FADD and/or caspase-8.
PEA15, a brain-specific phosphoprotein of unknown function
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