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Related Experiment Videos

A novel caspase-2 complex containing TRAF2 and RIP1.

Mohamed Lamkanfi1, Kathleen D'hondt, Lieselotte Vande Walle

  • 1Unit of Molecular Signalling and Cell Death, Department for Molecular Biomedical Research, Ghent University and Flemish Interuniversity Institute for Biotechnology, Technologiepark 927, Zwijnaarde B-9052, Belgium.

The Journal of Biological Chemistry
|December 14, 2004
PubMed
Summary

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Caspase-2 has a newly discovered nonenzymatic role in inducing NF-kappaB and p38 MAPK activation. This function is mediated by its caspase recruitment domain, independent of its proteolytic activity.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Immunology

Background:

  • Caspases are key enzymes in apoptosis and inflammation.
  • Caspase-2's known function is proteolytic in apoptosis.

Purpose of the Study:

  • To investigate a novel nonenzymatic function of caspase-2.
  • To elucidate the mechanism of caspase-2-mediated signaling.

Main Methods:

  • Protein interaction studies (TRAF1, TRAF2, RIP1).
  • Analysis of NF-kappaB and p38 MAPK activation.
  • Structure-function analysis of caspase-2 domains.

Main Results:

  • Caspase-2 induces NF-kappaB and p38 MAPK activation via TRAF2.
  • Caspase-2 forms a protein complex with TRAF2 and RIP1.

Related Experiment Videos

  • NF-kappaB and p38 MAPK activation is independent of caspase-2's enzymatic activity.
  • The caspase recruitment domain of caspase-2 is sufficient for activation.

    • Conclusions:

    • Caspase-2 possesses a novel nonenzymatic function.
    • Caspase-2 acts as an inducer of NF-kappaB and p38 MAPK pathways.
    • This function is mediated by a caspase-2, TRAF2, and RIP1 complex via the caspase recruitment domain.