Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B.

BCL10 belongs to the caspase recruitment domain (CARD) family of proteins that regulate apoptosis and NF-kappaB signaling pathways. Analysis of BCL10-deficient mice has revealed that BCL10 mediates NF-kappaB activation by antigen receptors in B and T cells. We recently identified a subclass of CARD proteins (CARD9, CARD11, and CARD14) that ...
may function to connect BCL10 to multiple upstream signaling pathways. We report here that CARD10 is a novel BCL10 interactor that belongs to the membrane-associated guanylate kinase family, a class of proteins that function to organize signaling complexes at plasma membranes. When expressed in cells, CARD10 binds to BCL10 and signals the activation of NF-kappaB through its N-terminal effector CARD domain. We propose that CARD10 functions as a molecular scaffold for the assembly of a BCL10 signaling complex that activates NF-kappaB.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Apoptosis Regulatory Proteins, Binding Sites, CARD Signaling Adaptor Proteins, Cell Line, Cell Membrane, Genes, Reporter, Guanylate Kinase, Humans, Mammals, Molecular Sequence Data, NF-kappa B, Neoplasm Proteins, Nucleoside-Phosphate Kinase, Organ Specificity, Sequence Alignment, Sequence Homology, Amino Acid, Signal Transduction, Transcription, Genetic, Transfection, src Homology Domains
J. Biol. Chem.
Date: Jun. 15, 2001
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