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

J Biol Chem. 2004 Aug 13;279(33):34323-31. doi: 10.1074/jbc.M402244200. Epub 2004 Jun 7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Apoptosis Regulatory Proteins
  • B-Cell CLL-Lymphoma 10 Protein
  • B-Lymphocytes / metabolism
  • CARD Signaling Adaptor Proteins
  • Cell Line
  • Cell Membrane / metabolism
  • Chromatography, Gel
  • Gene Library
  • Genes, Dominant
  • Guanylate Cyclase / chemistry
  • Guanylate Cyclase / metabolism*
  • Humans
  • I-kappa B Kinase
  • Immunoblotting
  • Jurkat Cells
  • Luciferases / metabolism
  • Lymphocytes / metabolism
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • NF-kappa B / metabolism*
  • Neoplasm Proteins / metabolism
  • Nucleoside-Phosphate Kinase / chemistry
  • Nucleoside-Phosphate Kinase / metabolism*
  • Plasmids / metabolism
  • Precipitin Tests
  • Protein Binding
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • T-Lymphocytes / metabolism
  • Transcription, Genetic
  • Two-Hybrid System Techniques

Substances

  • Adaptor Proteins, Signal Transducing
  • Apoptosis Regulatory Proteins
  • B-Cell CLL-Lymphoma 10 Protein
  • BCL10 protein, human
  • CARD Signaling Adaptor Proteins
  • CARD10 protein, human
  • Membrane Proteins
  • NF-kappa B
  • Neoplasm Proteins
  • Recombinant Proteins
  • Luciferases
  • Protein Serine-Threonine Kinases
  • CHUK protein, human
  • I-kappa B Kinase
  • IKBKB protein, human
  • IKBKE protein, human
  • Nucleoside-Phosphate Kinase
  • CARD11 protein, human
  • Guanylate Cyclase