Cell
Volume 81, Issue 4, 19 May 1995, Pages 505-512
Journal home page for Cell

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

https://doi.org/10.1016/0092-8674(95)90071-3Get rights and content
Under an Elsevier user license
open archive

Abstract

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 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 interieukin-lβ-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.

Cited by (0)

The first two authors contributed equally to this work.