Gene interactions and pathways from curated databases and text-mining

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CARD9 — NFKB1

Pathways - manually collected, often from reviews:

  • KEGG Tuberculosis: Complex of BCL10-CARD9-MALT1 → NFKB1/RELA (protein-protein, activation)

Text-mined interactions from Literome

Koseki et al., J Biol Chem 1999 : Point mutations in highly conserved residues in the CARD of CIPER disrupted the ability of CIPER to activate NF-kappaB and to form homodimers, indicating that the CARD is essential for NF-kappaB activation and dimerization
Bertin et al., J Biol Chem 2000 : CARD9 is a novel caspase recruitment domain containing protein that interacts with BCL10/CLAP and activates NF-kappa B ... When expressed in cells, CARD9 binds to BCL10 and activates NF-kappaB ... When expressed in cells, CARD9 binds to BCL10 and activates NF-kappaB ... We propose here that CARD9 is an upstream activator of BCL10 and NF-kappaB signaling
Bertin et al., J Biol Chem 2001 : When expressed in cells, CARD11 and CARD14 activate NF-kappaB and induce the phosphorylation of BCL10
Gross et al., Nature 2006 : Card9 couples to Bcl10 and regulates Bcl10-Malt1 mediated NF-kappaB activation induced by zymosan
Fontalba et al., J Immunol 2007 (Arthritis, Rheumatoid) : Thus, CARD8 may control NF-kappaB activation through a regulatory loop
Hara et al., J Immunol 2008 : Cell type-specific regulation of ITAM mediated NF-kappaB activation by the adaptors, CARMA1 and CARD9 ... Although the caspase recruitment domain (CARD)9-Bcl10 complex is essential for FcRgamma/DAP12 mediated NF-kappaB activation in myeloid cells, its involvement in NK cell receptor signaling is unknown
Goodridge et al., J Immunol 2009 : A recent report identified a role for CARD9 in innate anti-fungal responses, demonstrating CARD9-Bcl10 mediated activation of NF-kappaB and proinflammatory cytokine induction in murine bone marrow derived DC stimulated via Dectin-1
Bi et al., J Biol Chem 2010 : However, the molecular mechanism by which CARD9 mediates C. albicans induced NF-kappaB activation is not fully characterized ... Here we demonstrate that CARD9 is involved in mediating NF-kappaB activation induced by the hyphal form of C. albicans hyphae ( Hyphae ) but not by its heat inactivated unicellular form ... Finally, we find that although both CARD9 and Syk are required for Hyphae induced NF-kappaB activation, they regulate different signaling events in which CARD9 mediates IkappaBalpha kinase ubiquitination, whereas Syk regulates IkappaBalpha kinase phosphorylation ... Together, our data demonstrated that CARD9 is selectively involved in Dectin-2 induced NF-kappaB activation in response to C. albicans hyphae challenging