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CARD10 Is a Novel Caspase Recruitment Domain/Membrane-associated Guanylate Kinase Family Member That Interacts with BCL10 and Activates NF-κB

2001; Elsevier BV; Volume: 276; Issue: 24 Linguagem: Inglês

10.1074/jbc.m102488200

1083-351X

Lin Wang, Yin Guo, Waan-Jeng Huang, Xiaoling Ke, Jean‐Luc Poyet, Gulam A. Manji, Sarah Merriam, M.Alexandra Glucksmann, Peter S. DiStefano, Emad S. Alnemri, John Bertin,

Signaling Pathways in Disease

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.