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Gene Review

CARD11  -  caspase recruitment domain family, member 11

Homo sapiens

Synonyms: BENTA, BIMP3, CARD-containing MAGUK protein 1, CARMA1, Carma 1, ...
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Disease relevance of CARD11

  • The expression levels of CARMA1 and BCL10 were examined immunohistochemically in 30 patients with lymphoma [1].
  • RESULTS: CARMA1 mRNA was detected in 55% of lymphoma patients but in only 17% of chronic gastritis patients [1].
  • In addition, CARMA1 expression was positive more frequently in patients of DLBL without MALT lymphoma (100%) than in patients of MALT lymphoma (51%) [1].
  • The expression of CARMA1 and CARD9 was frequent in the Helicobacter pylori-negative patients (100% and 86%, respectively), in the API2-MALT1 chimeric transcript-positive patients (100% and 100%, respectively), and in the specimens from patients who did not respond to H. pylori eradication (76% and 71%, respectively) [1].

High impact information on CARD11

  • Phosphorylation of CARMA1: the link(er) to NF-kappaB activation [2].
  • CARMA1 mediates T cell receptor (TCR)-induced NF-kappaB activation [3].
  • Furthermore, PKCbeta interacted with the serine-rich CARMA1 linker, and both PKCbeta and PKCtheta phosphorylated identical serine residues (S564, S649, and S657) within this linker [4].
  • Our results indicate that the PKCtheta-induced phosphorylation of CARMA1 likely occurs on Ser552 on the Linker region of CARMA1 [3].
  • Along with reports that the CARMA1 MAGUK scaffold protein coordinates activation of Jnk and NF-kappaB but not of p38 or NFAT, our findings identify MAGUK scaffold proteins as 'orchestrators' of TCR signal specificity [5].

Biological context of CARD11


Anatomical context of CARD11

  • 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 [10].
  • CARMA1 plays a critical role in mediating activation of the NFkappaB transcription factor following antigen receptor stimulation of both B and T lymphocytes [11].
  • Carma1 is predominantly expressed in lymphocytes and represents a new member of the membrane-associated guanylate kinase family [7].
  • CONCLUSIONS: The overexpression of CARMA1 and CARD9 presumably is associated with the development or progression of gastric B-cell lymphoma, especially among patients who have disease in which the pathogenesis is not related to H. pylori [1].
  • Given that CARMA1 is specifically expressed in lymphoid tissues, could pharmacological inhibitors be designed to inhibit CARMA1's (or PKCtheta's) ability to promote the activation of NF-kappaB [12]?

Physical interactions of CARD11

  • CARMA1 interacts with Bcl10 via its caspase-recruitment domain (CARD) [13].
  • We also demonstrated that the cytoplasmic tail of CD26 interacts with CARMA1 in T-cells, resulting in signaling events that lead to NF-kappaB activation [14].

Regulatory relationships of CARD11


Other interactions of CARD11

  • These findings suggest that CARD11 and CARD14 are novel MAGUK family members that function as upstream activators of BCL10 and NF-kappaB signaling [10].
  • Physical and functional interaction of CARMA1 and CARMA3 with Ikappa kinase gamma-NFkappaB essential modulator [11].
  • CARMA proteins are scaffold molecules that contain a caspase recruitment domain and a membrane-associated guanylate kinase-like domain [11].
  • CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation [13].
  • Together, these results indicate that CARMA1 mediates CD3/CD28 costimulation-induced NF-kappaB activation by recruiting downstream signaling components into the immunological synapse [15].

Analytical, diagnostic and therapeutic context of CARD11


  1. Overexpression of caspase recruitment domain (CARD) membrane-associated guanylate kinase 1 (CARMA1) and CARD9 in primary gastric B-cell lymphoma. Nakamura, S., Nakamura, S., Matsumoto, T., Yada, S., Hirahashi, M., Suekane, H., Yao, T., Goda, K., Iida, M. Cancer (2005) [Pubmed]
  2. Phosphorylation of CARMA1: the link(er) to NF-kappaB activation. Rueda, D., Thome, M. Immunity (2005) [Pubmed]
  3. Phosphorylation of CARMA1 plays a critical role in T Cell receptor-mediated NF-kappaB activation. Matsumoto, R., Wang, D., Blonska, M., Li, H., Kobayashi, M., Pappu, B., Chen, Y., Wang, D., Lin, X. Immunity (2005) [Pubmed]
  4. Phosphorylation of the CARMA1 linker controls NF-kappaB activation. Sommer, K., Guo, B., Pomerantz, J.L., Bandaranayake, A.D., Moreno-García, M.E., Ovechkina, Y.L., Rawlings, D.J. Immunity (2005) [Pubmed]
  5. Scaffold protein Dlgh1 coordinates alternative p38 kinase activation, directing T cell receptor signals toward NFAT but not NF-kappaB transcription factors. Round, J.L., Humphries, L.A., Tomassian, T., Mittelstadt, P., Zhang, M., Miceli, M.C. Nat. Immunol. (2007) [Pubmed]
  6. CARD11 mediates factor-specific activation of NF-kappaB by the T cell receptor complex. Pomerantz, J.L., Denny, E.M., Baltimore, D. EMBO J. (2002) [Pubmed]
  7. Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation. Gaide, O., Martinon, F., Micheau, O., Bonnet, D., Thome, M., Tschopp, J. FEBS Lett. (2001) [Pubmed]
  8. A requirement for CARMA1 in TCR-induced NF-kappa B activation. Wang, D., You, Y., Case, S.M., McAllister-Lucas, L.M., Wang, L., DiStefano, P.S., Nuñez, G., Bertin, J., Lin, X. Nat. Immunol. (2002) [Pubmed]
  9. The CARMA1 signalosome links the signalling machinery of adaptive and innate immunity in lymphocytes. Rawlings, D.J., Sommer, K., Moreno-Garc??a, M.E. Nat. Rev. Immunol. (2006) [Pubmed]
  10. 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. Bertin, J., Wang, L., Guo, Y., Jacobson, M.D., Poyet, J.L., Srinivasula, S.M., Merriam, S., DiStefano, P.S., Alnemri, E.S. J. Biol. Chem. (2001) [Pubmed]
  11. Physical and functional interaction of CARMA1 and CARMA3 with Ikappa kinase gamma-NFkappaB essential modulator. Stilo, R., Liguoro, D., Di Jeso, B., Formisano, S., Consiglio, E., Leonardi, A., Vito, P. J. Biol. Chem. (2004) [Pubmed]
  12. Determining the destiny of NF-kappa B after TCR ligation: it's CARMA1. Bunnell, S.C. Mol. Interv. (2002) [Pubmed]
  13. CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation. Gaide, O., Favier, B., Legler, D.F., Bonnet, D., Brissoni, B., Valitutti, S., Bron, C., Tschopp, J., Thome, M. Nat. Immunol. (2002) [Pubmed]
  14. Caveolin-1 Triggers T-cell Activation via CD26 in Association with CARMA1. Ohnuma, K., Uchiyama, M., Yamochi, T., Nishibashi, K., Hosono, O., Takahashi, N., Kina, S., Tanaka, H., Lin, X., Dang, N.H., Morimoto, C. J. Biol. Chem. (2007) [Pubmed]
  15. CD3/CD28 costimulation-induced NF-kappaB activation is mediated by recruitment of protein kinase C-theta, Bcl10, and IkappaB kinase beta to the immunological synapse through CARMA1. Wang, D., Matsumoto, R., You, Y., Che, T., Lin, X.Y., Gaffen, S.L., Lin, X. Mol. Cell. Biol. (2004) [Pubmed]
  16. CARMA: A platform for analyzing microarray datasets that incorporate replicate measures. Greer, K.A., McReynolds, M.R., Brooks, H.L., Hoying, J.B. BMC Bioinformatics (2006) [Pubmed]
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