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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.

Pubmed ID: 8565075

Authors

  • Hsu H
  • Shu HB
  • Pan MG
  • Goeddel DV

Journal

Cell

Publication Data

January 26, 1996

Associated Grants

None

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