Related Experiment Video

Updated: May 7, 2026

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex
07:17

Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex

Published on: August 2, 2021

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

B Z Stanger1, P Leder, T H Lee

  • 1Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.

Cell
|May 19, 1995
PubMed

Insights

Researchers identified a novel protein, receptor interacting protein (RIP), that interacts with the Fas receptor and induces programmed cell death (apoptosis). This discovery sheds light on the molecular mechanisms of cell death signaling pathways.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Immunology

Background:

  • Fas/APO-1 (CD95) receptor ligation triggers programmed cell death.
  • Understanding the intracellular signaling pathways of Fas is crucial for cell death research.

Purpose of the Study:

  • To identify proteins interacting with the intracellular domain of the Fas receptor.
  • To characterize the function and properties of novel Fas-interacting proteins.

Main Methods:

  • Yeast two-hybrid system for protein-protein interaction screening.
  • Co-immunoprecipitation and Western blotting to confirm interactions.
  • Transient transfection and morphological analysis to assess apoptosis induction.

Main Results:

  • Identified a novel 74 kDa protein, receptor interacting protein (RIP), that binds to the Fas intracellular domain.
  • RIP also interacts with tumor necrosis factor receptor 1 (TNFR1) and contains a death domain.
  • Overexpression of RIP induces apoptosis in transfected cells.

Conclusions:

  • RIP is a novel protein that mediates Fas-induced apoptosis.
  • RIP plays a significant role in programmed cell death pathways.
  • RIP represents a new class of apoptosis-inducing proteins.

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