This entry includes animal B-cell lymphoma/leukemia 10 (BCL10) and Equine herpesvirus protein E10.In lymphoid cells BCL10 plays a critical role in the activation of the transcription factor nuclear factor kappa B (NF-kB) downstream of a variety of immune receptors, including the TCR, B cell receptor, NK-cell receptors, C type family lectin receptors, Ig family receptors and G protein-coupled receptors [, , ]. Activation of NF-kB through receptor-mediated pathways requires BCL10 to form a complex (known as CBM) with the paracaspase MALT1 and with CARD-containing adaptor protein CARMA []. BCL10 is involved in the regulation of apoptosis; a BCL10 gene tanslocation is found in mucosa-associated lymphoid tissue (MALT) lymphomas [, ]. BCL10 is involved in the adaptive and innate immune response [, ]. Equine herpesvirus protein E10 (v-E10) is the viral homologue of the BCL10 protein []. It induces membrane recruitment of cellular BCL10, and this induces TRAF-mediated NF-kappaB activation [].
Caspase recruiment domain-containing proteins (CARDs) are death domains (DDs) found associated with caspases []. They are known to be important in the signalling pathways for apoptosis, inflammation, and host-defense mechanisms [].This entry includes the Caspase-recruitment domain-containing protein 19 (CARD19), also known as Bcl10-interacting protein with CARD (BinCARD) which interacts with apoptosis inducer CARD protein Bcl10 through CARD. It inhibits Bcl10-mediated activation of NF-kappa B and to suppress Bcl10 phosphorylation [].
This entry represents the CARD domain found in BinCARD, also known as CARD19. BinCARD interacts with apoptosis inducer CARD protein Bcl10 through CARD. It inhibits Bcl10-mediated activation of NF-kappa B and to suppress Bcl10 phosphorylation [].In general, CARDs are death domains (DDs) found associated with caspases []. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms []. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes [].
This entry represents the CARD domain found in B-cell lymphoma/leukemia 10 (BCL10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction [, ].In general, CARDs are death domains (DDs) found associated with caspases []. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms []. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes [].
This entry represents the CARD domain found in CARD9, which is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages []. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction [].In general, CARDs are death domains (DDs) found associated with caspases []. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms []. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes [].
This entry represents the CARD domain found in CARD11, also known as CARMA1. CARMA1, together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), form the L-CBM signalosome (CBM complex in lymphoid immune cells) which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARMA1 associates with BCL10 via a CARD-CARD interaction [].In general, CARDs are death domains (DDs) found associated with caspases []. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms []. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes [].
The caspase recruitment domain (CARD) is a homotypic protein interaction module that participates in apoptosis signalling. This entry represents CARD11, which is a large multidomain scaffold protein that functions as upstream activator of NF-kappaB signalling []. It forms a CBM complex with BCL10 and MALT1. The CBM complex links AgR (antigen receptor) triggering to NF-kappaB activation []. Its activity is controlled by an Inhibitory Domain (ID) [].Mutations in the CARD11 gene cause B-cell expansion with NFKB and T-cell anergy (BENTA) []and Immunodeficiency 11 (IMD11) [].
