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Physical and functional interaction of CARMA1 and CARMA3 with Ikappa kinase gamma-NFkappaB essential modulator.

CARMA proteins are scaffold molecules that contain a caspase recruitment domain and a membrane-associated guanylate kinase-like domain. CARMA1 plays a critical role in mediating activation of the NFkappaB transcription factor following antigen receptor stimulation of both B and T lymphocytes. However, the biochemical mechanism by which CARMA1 regulates activation of NFkappaB remains to be determined. Here we have shown that CARMA1 and CARMA3 physically associate with Ikappa kinase gamma/NFkappaB essential modulator (IkappaKgamma-NEMO) in lymphoid and non-lymphoid cells. CARMA1 participates to an inducible large molecular complex that contains IkappaKgamma/NEMO, Bcl10, and IkappaKalpha/beta kinases. Expression of the NEMO-binding region of CARMA3 exerts a dominant negative effect on Bcl10-mediated activation of NFkappaB. Thus, our results provide direct evidence for physical and functional interaction between CARMA and the IkappaK complex and offer a biochemical framework to understand the molecular activities controlled by CARMA-1, -2, and -3 and Bcl10.

Pubmed ID: 15184390

Authors

  • Stilo R
  • Liguoro D
  • Di Jeso B
  • Formisano S
  • Consiglio E
  • Leonardi A
  • Vito P

Journal

The Journal of biological chemistry

Publication Data

August 13, 2004

Associated Grants

None

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Apoptosis Regulatory Proteins
  • B-Lymphocytes
  • CARD Signaling Adaptor Proteins
  • Cell Line
  • Cell Membrane
  • Chromatography, Gel
  • Gene Library
  • Genes, Dominant
  • Guanylate Cyclase
  • Humans
  • I-kappa B Kinase
  • Immunoblotting
  • Jurkat Cells
  • Luciferases
  • Lymphocytes
  • Membrane Proteins
  • NF-kappa B
  • Neoplasm Proteins
  • Nucleoside-Phosphate Kinase
  • Plasmids
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Recombinant Proteins
  • T-Lymphocytes
  • Transcription, Genetic
  • Two-Hybrid System Techniques