BCL10

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 these proteins:

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

References

References

1. (March 1999). "Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types". Cell.
2. "Entrez Gene: BCL10 B-cell CLL/lymphoma 10".
3. (April 2015). "Functional characterization of zebrafish. (Danio rerio) Bcl10". PLOS ONE.
4. (2018). "Ancient Origin of the CARD-Coiled Coil/Bcl10/MALT1-Like Paracaspase Signaling Complex Indicates Unknown Critical Functions". Frontiers in Immunology.
5. (June 2001). "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..
6. (April 2001). "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..
7. (Dec 2000). "CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B". J. Biol. Chem..
8. (2012). "Cutting edge: the "death" adaptor CRADD/RAIDD targets BCL10 and suppresses agonist-induced cytokine expression in T lymphocytes". J. Immunol..
9. (February 2008). "NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation". Proc. Natl. Acad. Sci. U.S.A..
10. (October 2000). "Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma". Mol. Cell.
11. (April 2000). "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem..