CARD9 Is a Novel Caspase Recruitment Domain-containing Protein That Interacts With BCL10/CLAP and Activates NF-κB
| Autor: | Michael D. Jacobson, Sarah Merriam, Martin J. S. Dyer, Lin Wang, John Bertin, Peter S. DiStefano, Keith E. Robison, Ming-Qing Du, Jean-Luc Poyet, Emad S. Alnemri, Srinivasa M. Srinivasula, Yin Guo |
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| Rok vydání: | 2000 |
| Předmět: |
Amino Acid Motifs
Molecular Sequence Data Apoptosis Endogeny Biochemistry Mice chemistry.chemical_compound medicine Animals Amino Acid Sequence Molecular Biology B cell Caspase Adaptor Proteins Signal Transducing biology Activator (genetics) NF-kappa B Proteins NF-κB Cell Biology B-Cell CLL-Lymphoma 10 Protein Molecular biology BCL10 medicine.anatomical_structure chemistry Caspases biology.protein Signal transduction |
| Zdroj: | Journal of Biological Chemistry. 275:41082-41086 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.c000726200 |
| Popis: | BCL10/CLAP is an activator of apoptosis and NF-kappaB signaling pathways and has been implicated in B cell lymphomas of mucosa-associated lymphoid tissue. Although its role in apoptosis remains to be determined, BCL10 likely activates NF-kappaB through the IKK complex in response to upstream stimuli. The N-terminal caspase recruitment domain (CARD) of BCL10 has been proposed to function as an activation domain that mediates homophilic interactions with an upstream CARD-containing NF-kappaB activator. To identify upstream signaling partners of BCL10, we performed a mammalian two-hybrid analysis and identified CARD9 as a novel CARD-containing protein that interacts selectively with the CARD activation domain of BCL10. When expressed in cells, CARD9 binds to BCL10 and activates NF-kappaB. Furthermore, endogenous CARD9 is found associated with BCL10 suggesting that both proteins form a pre-existing signaling complex within cells. CARD9 also self-associates and contains extensive coiled-coil motifs that may function as oligomerization domains. We propose here that CARD9 is an upstream activator of BCL10 and NF-kappaB signaling. |
| Databáze: | OpenAIRE |
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