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Laboratory of Molecular Biology, Flanders Interuniversity Institute for Biotechnology and University of Ghent, Ghent, Belgium
TNF-R55 is the main receptor mediating TNF-induced cytotoxicity.
However, in some cells TNF-R75 also signals cell death. In PC60 cells,
the presence of both receptor types is required to induce apoptosis
following either specific TNF-R55 or TNF-R75 triggering, pointing to a
mechanism of receptor cooperation. In this study, we extend previous
observations and show that TNF-R55 and TNF-R75 cooperation in the case
of apoptosis in PC60 cells is bidirectional. We also demonstrate
ligand-independent TNF-R55-mediated cooperation in TNF-R75-induced
granulocyte/macrophage-CSF secretion, but not vice versa. To determine
which part of the intracellular TNF-R75 sequence was responsible for
the observed receptor cooperation in apoptosis, we introduced different
TNF-R75 mutant constructs in PC60 cells already expressing TNF-R55. Our
data indicate that an intact TNF-R-associated factors 1 and 2
(TRAF1/TRAF2)-binding domain is required for receptor cooperation.
These findings suggest a role for the TRAF complex in TNF-R cooperation
in the induction of cell death in PC60 cells. Nevertheless,
introduction of a dominant negative (DN) TRAF2 molecule was not able to
affect receptor cooperation. Remarkably, TRAF2-DN overexpression, which
was found to inhibit the TNF-dependent recruitment of endogenous
wild-type TRAF2 to the TNF-R75 signaling complex, could neither block
TNF-R55- or TNF-R75-induced NF-
B activation nor
granulocyte/macrophage-CSF secretion. Possibly, additional factors
different from TRAF2 are involved in TNF-mediated NF-B activation.
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