Cell. 1995 May 19;81(4):513-23.

RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death.External

Stanger, B. Z., Leder, P., Lee, T. H., Kim, E., Seed, B.,
--- - Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Ligation of the extracellular domain of the cell surface receptor Fas/APO-1 (CD95) 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 Fas: Fas itself, and a novel 74 kDa protein we have named RIP, for receptor interacting protein. RIP also interacts weakly with the p55 tumor necrosis factor receptor (TNFR1) intracellular domain, but not with a mutant version of Fas corresponding to the murine lprcg mutation. RIP contains an N-terminal region with homology to protein kinases and a C-terminal region containing a cytoplasmic motif (death domain) present in the Fas and TNFR1 intracellular domains. Transient overexpression of RIP causes transfected cells to undergo the morphological changes characteristic of apoptosis. Taken together, these properties indicate that RIP is a novel form of apoptosis-inducing protein.
PMID: 7538908External
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
In vitro interaction
  DD1 DD2 Reference
Family DD1 DD2 Method Species Region Expression Species Region Expression
DD Fas Link Fas Yeast two-hybrid Human 192-329 Yeast Human Full length Yeast 7538908
DD Fas Link RIP Yeast two-hybrid Human 192-329 Yeast Human Full length Yeast 7538908
(Link: click this icon to show interactions only between the two corresponding DDs)