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J Biol Chem, Vol. 274, Issue 29, 20127-20132, July 16, 1999
B
,
From the Members of the tumor necrosis factor receptor
superfamily induce apoptosis via interaction with FADD and regulate
cell growth and differentiation through TRADD and TRAFs molecules.
While screening for molecules involved in the regulation of death
receptor signaling, we identified a novel protein, c-E10. c-E10
contains an amino-terminal caspase-recruiting domain (CARD) and shares
a sequence homologous with E10, a viral CARD-containing protein that
binds to c-E10. In transfection experiments c-E10 oligomerizes, binds
to the cytoplasmic portion of TRAIL receptor 1 (DR4) and coprecipitates
with TRADD. Expression of c-E10 under the control of a
doxycycline-dependent transcriptional transactivator
results in NF- Fondazione A. Cesalpino, I Clinica Medica,
V.le Policlinico 155, 00161 Roma, Italy and § Basel
Institute for Immunology, Grenzacherstrasse 487, Postfach CH-4005,
Basel, Switzerland
B activation, which is inhibited by dominant negative
forms of TRAF2 and NIK kinase. Thus, our results suggest that c-E10 is
an adapter protein that activates NF-B through a molecular pathway
involved in death receptor signaling.
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