• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

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

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.

Pubmed ID: 7538908

Authors

  • Stanger BZ
  • Leder P
  • Lee TH
  • Kim E
  • Seed B

Journal

Cell

Publication Data

May 19, 1995

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK43031

Mesh Terms

  • Amino Acid Sequence
  • Antigens, CD
  • Antigens, CD95
  • Antigens, Surface
  • Apoptosis
  • Base Sequence
  • Binding Sites
  • Cloning, Molecular
  • Gene Deletion
  • Molecular Sequence Data
  • Proteins
  • Receptors, Tumor Necrosis Factor
  • Receptors, Tumor Necrosis Factor, Type I
  • Saccharomyces cerevisiae