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Validated All-in-One™ qPCR Primer for CARD11(NM_001324281.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene belongs 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. This protein is also a member of the CARD protein family, which is defined by carrying a characteristic caspase-associated recruitment domain (CARD). This protein has a domain structure similar to that of CARD14 protein. The CARD domains of both proteins have been shown to specifically interact with BCL10, a protein known to function as a positive regulator of cell apoptosis and NF-kappaB activation. When expressed in cells, this protein activated NF-kappaB and induced the phosphorylation of BCL10.
Gene References into function
- CARMA1 is an essential signaling component that mediates TCR-induced NF-kappa B activation.
- CARMA1 is a critical lipid raft-associated regulator of TCR-induced NF-kappa B activation and CD28 costimulation-dependent Jnk activation.
- CARD11 mediates factor-specific activation of NF-kappaB by the T cell receptor complex
- CARMA1 and CARMA3 bind to Ikappa kinase gamma-NFkappaB in B and T lymphocytes
- Phosphorylation of CARMA1 plays a critical role in T Cell receptor-mediated NF-kappaB activation.
- CARMA1 complex is required for induction of NF-kappaB by Akt
- These findings suggest that endogenous Nore1B recruits active Ras to the APC-T cell interface and mediates the interaction between Ras and Carma1.
- CaMKII phosphorylates CARMA1 on Ser109 and that the phosphorylation facilitates the interaction between CARMA1 and Bcl10.
- CD26 interacts with CARMA1 in T-cells, resulting in signaling events that lead to activation.
- oligomerization of CARMA1 is through its Coiled-coil domain. Disruption of the predicted structure of the Coiled-coil domain of CARMA1 impaired its oligomerization and, importantly, abrogated CARMA1-mediated NF-kappaB activation
- H-RS cells show a deregulated B cell programme 8 lacking expression of the lymphocyte specific CARMA1 protein.
- results demonstrate that CARD11 is a bona fide oncogene in diffuse large B cell lymphoma
- Data show that the protein kinase C-responsive inhibitory domain of CARD11 functions in NF-kappaB activation to regulate the association of multiple signaling cofactors that differentially depend on Bcl10 and MALT1 for association.
- NF-kappaB pathway activation by CARD11 or tumor necrosis factor-alpha, compensatory IKKalpha activity was also observed with IKKbeta