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Product Reference
FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis.
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| Author |
Chinnaiyan, A M, et al. |
| Citation Information |
Cell, 81: 505-12 (1995), : (1995) |
| Related Products |
05-486, 06-711 |
| Pub Med ID |
7538907 |
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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.
