TI  -  <prot>FADD</prot> , a novel death domain-containing protein, interacts with the death
      domain of  <prot>Fas</prot>  and initiates apoptosis.
PG  - 505-12
AB  - Using the cytoplasmic domain of <prot>Fas</prot> in the yeast two-hybrid system, we
      have identified a novel interacting protein,   <prot>FADD</prot>  , which binds  <prot>Fas</prot>  and
       <prot>Fas</prot>-<prot>FD5</prot> , a mutant of <prot>Fas</prot> possessing enhanced killing activity, but not the
      functionally inactive mutants <prot>Fas</prot>-<prot>LPR</prot> and <prot>Fas</prot>-<prot>FD8</prot>. <prot>FADD</prot> contains a death
      domain homologous to the death domains of <prot>Fas</prot> and <prot>TNFR-1</prot>. A point mutation
      in  <prot>FADD</prot> , analogous to the lpr mutation of <prot>Fas</prot>, abolishes its ability to
      bind  <prot>Fas</prot> , suggesting a death domain to death domain interaction.
      Overexpression of  <prot>FADD</prot>  in MCF7 and BJAB cells induces apoptosis, which,
      like <prot>Fas</prot>-induced apoptosis, is blocked by  <prot>CrmA</prot> , a specific inhibitor of
      the  <prot><prot>interleukin-1 beta</prot> -converting enzyme</prot>. These findings suggest that <prot>FADD</prot>
      may play an important role in the proximal signal transduction of <prot>Fas</prot>.
AD  - Department of Pathology, University of Michigan Medical School, Ann Arbor
