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Regulation of NF-kappaB-dependent lymphocyte activation and development by paracaspase.

Paracaspase (MALT1), a member of an evolutionarily conserved superfamily of caspase-like proteins, has been shown to bind and colocalize with the protein Bcl10 in vitro and, because of this association, has been suggested to be involved in the CARMA1-Bcl10 pathway of antigen-induced nuclear factor kappaB (NF-kappaB) activation. We demonstrate that primary T and B lymphocytes from paracaspase-deficient mice are defective in antigen-receptor-induced NF-kappaB activation, cytokine production, and proliferation. Paracaspase acts downstream of Bcl10 to induce NF-kappaB activation and is required for the normal development of B cells, indicating that paracaspase provides the missing link between Bcl10 and activation of the IkappaB kinase complex.

Pubmed ID: 14576442


  • Ruefli-Brasse AA
  • French DM
  • Dixit VM


Science (New York, N.Y.)

Publication Data

November 28, 2003

Associated Grants


Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Antibody Formation
  • Antigens, CD
  • B-Lymphocyte Subsets
  • B-Lymphocytes
  • Caspases
  • Cell Differentiation
  • Cell Division
  • Cell Survival
  • Cells, Cultured
  • Cytokines
  • Gene Deletion
  • Gene Targeting
  • Guanylate Kinase
  • I-kappa B Kinase
  • Lymphocyte Activation
  • Lymphoma, B-Cell, Marginal Zone
  • Mice
  • Mice, Inbred C57BL
  • NF-kappa B
  • Neoplasm Proteins
  • Nucleoside-Phosphate Kinase
  • Phosphorylation
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Receptors, Antigen, B-Cell
  • Receptors, Antigen, T-Cell
  • Signal Transduction
  • T-Lymphocyte Subsets
  • T-Lymphocytes
  • Transfection