FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
Cell, 1995•cell.com
Using the cytoplasmic domain of Fas in the yeast twohybrid system, we have identified a
novel interacting protein, FADD, which binds Fasand 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 Ipr mutation of Fas, abolishes its ability to bind
Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in …
novel interacting protein, FADD, which binds Fasand 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 Ipr mutation of Fas, abolishes its ability to bind
Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in …
Summary
Using the cytoplasmic domain of Fas in the yeast twohybrid system, we have identified a novel interacting protein, FADD, which binds Fasand 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 Ipr 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-1fMonverting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.
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