TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.

Tumor necrosis factor (TNF) can induce apoptosis and activate NF-kappa B through signaling cascades emanating from TNF receptor 1 (TNFR1). TRADD is a TNFR1-associated signal transducer that is involved in activating both pathways. Here we show that TRADD directly interacts with TRAF2 and FADD, signal transducers that activate NF-kappa B ...
and induce apoptosis, respectively. A TRAF2 mutant lacking its N-terminal RING finger domain is a dominant-negative inhibitor of TNF-mediated NF-kappa B activation, but does not affect TNF-induced apoptosis. Conversely, a FADD mutant lacking its N-terminal 79 amino acids is a dominant-negative inhibitor of TNF-induced apoptosis, but does not inhibit NF-kappa B activation. Thus, these two TNFR1-TRADD signaling cascades appear to bifurcate at TRADD.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Antigens, CD, Apoptosis, Carrier Proteins, Cell Line, Fas-Associated Death Domain Protein, Humans, Interleukin-1, Mice, Molecular Sequence Data, NF-kappa B, Proteins, Receptors, Tumor Necrosis Factor, Receptors, Tumor Necrosis Factor, Type I, Sequence Deletion, Signal Transduction, TNF Receptor-Associated Death Domain Protein, TNF Receptor-Associated Factor 1, TNF Receptor-Associated Factor 2, Transcriptional Activation, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins, Tumor Necrosis Factor-alpha
Cell
Date: Jan. 26, 1996
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