Biology:BCL10

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

B-cell lymphoma/leukemia 10 is a protein that in humans is encoded by the BCL10 gene. Like BCL2, BCL3, BCL5, BCL6, BCL7A, and BCL9, it has clinical significance in lymphoma.

Function

Bcl10 was identified by its translocation in a case of mucosa-associated lymphoid tissue (MALT) lymphoma. The protein encoded by this gene contains a caspase recruitment domain (CARD), and has been shown to activate NF-κB. This protein is reported to interact with other CARD and coiled coil domain containing proteins including CARD9, -10, -11 and -14, which are thought to function as upstream regulators in NF-κB signaling. This protein is found to form a complex with the paracaspase MALT1, a protein encoded by another gene known to be translocated in MALT lymphoma. MALT1 and Bcl10 thought to synergize in the activation of NF-κB, and the deregulation of either of them may contribute to the same pathogenetic process that leads to the malignancy. Bcl10 is evolutionary conserved since cnidaria and has been shown to be functionally conserved all the way back to zebrafish. Notably, just like the upstream CARD-CC family, Bcl10 is absent in insects and nematodes, and the correlated phylogenetic distribution of Bcl10 and CARD-CC proteins indicate a conserved complex.

Interactions

BCL10 has been shown to interact with:

• CARD10,
• CARD11,
• CARD14,
• CARD9
• CRADD,
• IKBKG,
• MALT1, and
• TRAF2.

External links

• Human BCL10 genome location and BCL10 gene details page in the UCSC Genome Browser.

Further reading

• "Genetic alterations underlying the pathogenesis of MALT lymphoma". Hematol. J. 3 (1): 10–3. 2003. doi:10.1038/sj.thj.6200146. PMID 11960389. 
• "Loss of heterozygosity analysis defines a critical region in chromosome 1p22 commonly deleted in human malignant mesothelioma". Cancer Res. 56 (19): 4297–301. 1996. PMID 8813110. 
• "CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10". J. Biol. Chem. 274 (15): 9955–9961. 1999. doi:10.1074/jbc.274.15.9955. PMID 10187770. 
• "Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase". J. Biol. Chem. 274 (15): 9962–9968. 1999. doi:10.1074/jbc.274.15.9962. PMID 10187771. 
• "mE10, a novel caspase recruitment domain-containing proapoptotic molecule". J. Biol. Chem. 274 (15): 10287–10292. 1999. doi:10.1074/jbc.274.15.10287. PMID 10187815. 
• "Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32)". Nat. Genet. 22 (1): 63–68. 1999. doi:10.1038/8767. PMID 10319863. 
• "CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis". J. Biol. Chem. 274 (25): 17946–17954. 1999. doi:10.1074/jbc.274.25.17946. PMID 10364242. 
• "Absence of BCL10 mutations in human malignant mesothelioma". Cell 97 (6): 684–686. 1999. doi:10.1016/S0092-8674(02)09765-9. PMID 10380921. 
• "c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and activates nuclear factor-kappaB". J. Biol. Chem. 274 (29): 20127–20132. 1999. doi:10.1074/jbc.274.29.20127. PMID 10400625. 
• "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem. 275 (15): 11114–11120. 2000. doi:10.1074/jbc.275.15.11114. PMID 10753917. 
• "BCL10 expression in normal and neoplastic lymphoid tissue. Nuclear localization in MALT lymphoma". Am. J. Pathol. 157 (4): 1147–1154. 2000. doi:10.1016/S0002-9440(10)64630-5. PMID 11021819. 
• "CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B". J. Biol. Chem. 275 (52): 41082–41086. 2001. doi:10.1074/jbc.C000726200. PMID 11053425. 
• "Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma". Mol. Cell 6 (4): 961–967. 2000. doi:10.1016/S1097-2765(05)00086-9. PMID 11090634. 
• "vCLAP, a caspase-recruitment domain-containing protein of equine Herpesvirus-2, persistently activates the Ikappa B kinases through oligomerization of IKKgamma". J. Biol. Chem. 276 (5): 3183–3187. 2001. doi:10.1074/jbc.C000792200. PMID 11113112. 
• "Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure". Cell 104 (1): 33–42. 2001. doi:10.1016/S0092-8674(01)00189-1. PMID 11163238. 
• "Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B". J. Biol. Chem. 276 (24): 21405–21409. 2001. doi:10.1074/jbc.M102488200. PMID 11259443. 
• "Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-kappa B signaling pathway". J. Biol. Chem. 276 (22): 19012–19019. 2001. doi:10.1074/jbc.M009984200. PMID 11262391. 
• "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". J. Biol. Chem. 276 (15): 11877–11882. 2001. doi:10.1074/jbc.M010512200. PMID 11278692. 
• "Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation". FEBS Lett. 496 (2–3): 121–127. 2001. doi:10.1016/S0014-5793(01)02414-0. PMID 11356195.