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CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B.

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.

Pubmed ID: 11053425

Authors

  • Bertin J
  • Guo Y
  • Wang L
  • Srinivasula SM
  • Jacobson MD
  • Poyet JL
  • Merriam S
  • Du MQ
  • Dyer MJ
  • Robison KE
  • DiStefano PS
  • Alnemri ES

Journal

The Journal of biological chemistry

Publication Data

December 29, 2000

Associated Grants

  • Agency: NCI NIH HHS, Id: CA85421

Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Caspases
  • Mice
  • Molecular Sequence Data
  • NF-kappa B
  • Proteins