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Related Experiment Videos

RIP3, a novel apoptosis-inducing kinase.

X Sun1, J Lee, T Navas

  • 1Departments of Molecular Oncology, Genentech, Inc., South San Francisco, California 94080, USA.

The Journal of Biological Chemistry
|June 8, 1999
PubMed
Summary

Receptor-interacting protein 3 (RIP3) binds RIP and inhibits TNF-induced NF-kappaB activation. RIP3 also potently induces apoptosis by binding initiator caspases.

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Area of Science:

  • Molecular biology
  • Cell signaling
  • Apoptosis research

Background:

  • Receptor-interacting protein (RIP) and RIP2 are known signaling molecules.
  • RIP has a C-terminal death domain, while RIP2 has a caspase activation and recruitment domain.
  • RIP3 possesses a unique C-terminal domain distinct from RIP and RIP2.

Purpose of the Study:

  • To characterize the novel gene product RIP3.
  • To investigate RIP3's interaction with RIP and its role in tumor necrosis factor (TNF) signaling.
  • To determine RIP3's function in apoptosis and NF-kappaB activation.

Main Methods:

  • Homology analysis of kinase domains.
  • Interaction studies between RIP3 and RIP.
  • Analysis of RIP3's effect on TNF receptor-1 signaling complex.
  • Overexpression studies to assess apoptosis induction and caspase binding.

Main Results:

  • RIP3 shares homology with RIP and RIP2 but has a unique C terminus.
  • RIP3 binds to RIP via its C-terminal segment and is recruited to the TNF receptor-1 complex.
  • RIP3 attenuates RIP and TNF receptor-1-induced NF-kappaB activation.
  • RIP3 overexpression potently induces apoptosis and binds large prodomain initiator caspases.

Conclusions:

  • RIP3 is a novel regulator of TNF signaling and apoptosis.
  • RIP3 acts as an inhibitor of NF-kappaB activation.
  • RIP3's unique C terminus is crucial for its function in apoptosis induction.

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