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*
Institute of Cell Biology and Immunology, University of Stuttgart, Stuttgart, Germany; and
Institute of Pathology, Universitätsklinikum Benjamin Franklin, Berlin, Germany
Costimulation of TNFR80 can strongly enhance TNFR60-induced cell
death. In this study, we show that this enhancement is TNFR60
selective, as neither TNF-related apoptosis-inducing ligand/Apo2
ligand-, Apo1/Fas-, ceramide-, nor daunorubicin-mediated cell death was
affected by costimulation of TNFR80. We further demonstrate that
TNFR-associated factor 2 (TRAF2) is critically involved in both
negative and positive regulation of TNF-induced cell death.
Overexpression of TRAF2 and of a TRAF2 mutant, deficient in nuclear
factor-
B activation, selectively desensitized and enhanced,
respectively, TNFR60-induced cell death in HeLa cells. However, upon
costimulation of TNFR80, which mediates activation of nuclear
factor-B and the c-Jun amino-terminal kinase via TRAF2, TNF-induced
cell death is drastically enhanced in parental and TRAF2-transfected,
but not in TRAF2 (87–501)-transfected cells. These data point to a
critical role of TRAF2 in the apoptotic TNFR cross talk, whereby the
TNFR80-dependent enhancement of TNFR60-induced cell death is due to
TNFR80-mediated negative regulation of TRAF2 function(s). An
interference with TRAF2 function was confirmed independently by
analysis of c-Jun amino-terminal kinase activation via TNFR60 upon
prestimulation of TNFR80. We propose that the apoptotic TNFR cross talk
is based on TNFR80-mediated abrogation of antiapoptotic TRAF2-dependent
signaling pathways initiated by TNFR60, but not Apo1/Fas or the
apoptotic TNF-related apoptosis-inducing ligand
receptors.
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