| First Author | Wang L | Year | 2001 |
| Journal | J Biol Chem | Volume | 276 |
| Issue | 24 | Pages | 21405-9 |
| PubMed ID | 11259443 | Mgi Jnum | J:114026 |
| Mgi Id | MGI:3688036 | Doi | 10.1074/jbc.M102488200 |
| Citation | Wang L, et al. (2001) Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B. J Biol Chem 276(24):21405-9 |
| abstractText | 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. |
