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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. | ||
| Authors: | Chinnaiyan, A M, et al. | |
| Citation: | Cell, 81: 505-12 (1995) | |
| Pub Med ID: | 7538907 | |
| Year: | 1995 | |
| 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 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. | |
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