TI  -  <prot>RIP</prot> : a novel protein containing a death domain that interacts with
        <prot>Fas</prot> / <prot>APO-1</prot>  (<prot>CD95</prot>)  in yeast and causes cell death.
PG  - 513-23
AB  - Ligation of the extracellular domain of the cell surface receptor
      <prot>Fas</prot>/<prot>APO-1</prot> (<prot>CD95</prot>) elicits a characteristic programmed death response in
      susceptible cells. Using a genetic selection based on protein-protein
      interaction in yeast, we have identified two gene products that associate
      with the intracellular domain of   <prot>Fas</prot>  :  <prot>Fas</prot>  itself, and a novel 74 kDa
      protein we have named  <prot>RIP</prot> , for <prot>receptor interacting protein</prot>.  <prot>RIP</prot>  also
      interacts weakly with the  <prot>p55</prot> tumor necrosis factor receptor (<prot>TNFR1</prot>) 
      intracellular domain, but not with a mutant version of <prot>Fas</prot> corresponding
      to the murine lprcg mutation. <prot>RIP</prot> contains an N-terminal region with
      homology to protein kinases and a C-terminal region containing a
      cytoplasmic motif (death domain) present in the <prot>Fas</prot> and <prot>TNFR1</prot>
      intracellular domains. Transient overexpression of <prot>RIP</prot> causes transfected
      cells to undergo the morphological changes characteristic of apoptosis.
      Taken together, these properties indicate that <prot>RIP</prot> is a novel form of
      apoptosis-inducing protein.
AD  - Howard Hughes Medical Institute, Harvard Medical School, Boston,
