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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.

Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the lpr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interleukin-1 beta-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.

Pubmed ID: 7538907

Authors

  • Chinnaiyan AM
  • O'Rourke K
  • Tewari M
  • Dixit VM

Journal

Cell

Publication Data

May 19, 1995

Associated Grants

None

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Antigens, CD95
  • Antigens, Surface
  • Apoptosis
  • Base Sequence
  • Binding Sites
  • Carrier Proteins
  • Cell Line
  • Cloning, Molecular
  • Fas-Associated Death Domain Protein
  • Humans
  • Molecular Sequence Data
  • Point Mutation
  • Saccharomyces cerevisiae
  • Serpins
  • Signal Transduction
  • Viral Proteins