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CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B.

http://www.ncbi.nlm.nih.gov/pubmed/11278692

The caspase recruitment domain (CARD) is a protein-binding module that mediates the assembly of CARD-containing proteins into apoptosis and NF-kappaB signaling complexes. We report here that CARD protein 11 (CARD11) and CARD protein 14 (CARD14) are novel CARD-containing proteins that belong to the membrane-associated guanylate kinase (MAGUK) family, a class of proteins that functions as molecular scaffolds for the assembly of multiprotein complexes at specialized regions of the plasma membrane. CARD11 and CARD14 have homologous structures consisting of an N-terminal CARD domain, a central coiled-coil domain, and a C-terminal tripartite domain comprised of a PDZ domain, an Src homology 3 domain, and a GUK domain with homology to guanylate kinase. The CARD domains of both CARD11 and CARD14 associate specifically with the CARD domain of BCL10, a signaling protein that activates NF-kappaB through the IkappaB kinase complex in response to upstream stimuli. When expressed in cells, CARD11 and CARD14 activate NF-kappaB and induce the phosphorylation of BCL10. These findings suggest that CARD11 and CARD14 are novel MAGUK family members that function as upstream activators of BCL10 and NF-kappaB signaling.

Pubmed ID: 11278692 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Amino Acid Sequence | Apoptosis Regulatory Proteins | CARD Signaling Adaptor Proteins | Guanylate Cyclase | Guanylate Kinase | Membrane Proteins | Molecular Sequence Data | Multigene Family | NF-kappa B | Neoplasm Proteins | Nucleoside-Phosphate Kinase | Phosphorylation | Precipitin Tests | Protein Binding | Sequence Homology, Amino Acid

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Associated grants

  • Agency: NCI NIH HHS, Id: CA85421

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