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CARDINAL, a novel caspase recruitment domain protein, is an inhibitor of multiple NF-kappa B activation pathways

L Bouchier-Hayes1, H Conroy, H Egan

  • 1Molecular Cell Biology Laboratory, Department of Genetics, Smurfit Institute, Trinity College, Dublin 2, Ireland.

The Journal of Biological Chemistry
|September 12, 2001
PubMed

Insights

A novel protein, CARDINAL, regulates inflammatory signals by suppressing NF-kappaB activation. It interacts with IKKgamma (NEMO), offering a new target for controlling inflammation.

Area of Science:

  • Molecular Biology
  • Immunology
  • Cell Biology

Background:

  • Proteins with caspase recruitment domain (CARD) motifs are involved in apoptosis and inflammation.
  • NF-kappaB activation is crucial in inflammatory responses.

Purpose of the Study:

  • To identify and characterize a novel CARD-containing protein.
  • To investigate the role of CARDINAL in NF-kappaB signaling pathways.

Main Methods:

  • Protein identification and homology analysis.
  • Functional assays for apoptosis and NF-kappaB activation.
  • Co-immunoprecipitation to determine protein interactions.

Main Results:

  • CARDINAL, a novel CARD protein, was identified.
  • CARDINAL suppressed NF-kappaB activation induced by various inflammatory stimuli.
  • CARDINAL directly interacts with IKKgamma (NEMO).

Conclusions:

  • CARDINAL acts as a negative regulator of NF-kappaB signaling.
  • CARDINAL's interaction with IKKgamma provides a mechanism for its inhibitory function.
  • CARDINAL is a novel regulator of pro-inflammatory signals.

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