BCL10

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BCL10
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBCL10, CARMEN, CIPER, CLAP, c-E10, mE10, IMD37, B-cell CLL/lymphoma 10, B cell CLL/lymphoma 10, immune signaling adaptor, BCL10 immune signaling adaptor
External IDsOMIM: 603517 MGI: 1337994 HomoloGene: 2912 GeneCards: BCL10
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003921
NM_001320715

NM_009740

RefSeq (protein)

NP_001307644
NP_003912
NP_001307644.1

NP_033870

Location (UCSC)Chr 1: 85.27 – 85.28 MbChr 3: 145.63 – 145.64 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

B-cell lymphoma/leukemia 10 is a protein that in humans is encoded by the BCL10 gene.[5][6] 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.[6] Bcl10 is evolutionary conserved since cnidaria and has been shown to be functionally conserved all the way back to zebrafish.[7][8] 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:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142867 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028191 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Willis TG, Jadayel DM, Du MQ, Peng H, Perry AR, Abdul-Rauf M, Price H, Karran L, Majekodunmi O, Wlodarska I, Pan L, Crook T, Hamoudi R, Isaacson PG, Dyer MJ (March 1999). "Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types". Cell. 96 (1): 35–45. doi:10.1016/S0092-8674(00)80957-5. PMID 9989495. S2CID 1613152.
  6. ^ a b "Entrez Gene: BCL10 B-cell CLL/lymphoma 10".
  7. ^ Mazzone P, Scudiero I, Ferravante A, Paolucci M, D'Andrea LE, Varricchio E, Telesio G, De Maio C, Pizzulo M, Zotti T, Reale C, Vito P, Stilo R (April 2015). "Functional characterization of zebrafish. (Danio rerio) Bcl10". PLOS ONE. 10 (4): e0122365. Bibcode:2015PLoSO..1022365M. doi:10.1371/journal.pone.0122365. PMC 4388727. PMID 25849213.
  8. ^ Staal J, Driege Y, Haegman M, Borghi A, Hulpiau P, Lievens L, et al. (2018). "Ancient Origin of the CARD-Coiled Coil/Bcl10/MALT1-Like Paracaspase Signaling Complex Indicates Unknown Critical Functions". Frontiers in Immunology. 9: 1136. doi:10.3389/fimmu.2018.01136. PMC 5978004. PMID 29881386.
  9. ^ Wang L, Guo Y, Huang WJ, Ke X, Poyet JL, Manji GA, Merriam S, Glucksmann MA, DiStefano PS, Alnemri ES, Bertin J (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. 276 (24): 21405–9. doi:10.1074/jbc.M102488200. PMID 11259443.
  10. ^ a b Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, Alnemri ES (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. 276 (15): 11877–82. doi:10.1074/jbc.M010512200. PMID 11278692. S2CID 35815019.
  11. ^ Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, DiStefano PS, Alnemri ES (Dec 2000). "CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B". J. Biol. Chem. 275 (52): 41082–6. doi:10.1074/jbc.C000726200. PMID 11053425.
  12. ^ Lin Q, Liu Y, Moore DJ, Elizer SK, Veach RA, Hawiger J, Ruley HE (2012). "Cutting edge: the "death" adaptor CRADD/RAIDD targets BCL10 and suppresses agonist-induced cytokine expression in T lymphocytes". J. Immunol. 188 (6): 2493–7. doi:10.4049/jimmunol.1101502. PMC 3294148. PMID 22323537.
  13. ^ Wu CJ, Ashwell JD (February 2008). "NEMO recognition of ubiquitinated Bcl10 is required for T cell receptor-mediated NF-kappaB activation". Proc. Natl. Acad. Sci. U.S.A. 105 (8): 3023–8. Bibcode:2008PNAS..105.3023W. doi:10.1073/pnas.0712313105. PMC 2268578. PMID 18287044.
  14. ^ Uren AG, O'Rourke K, Aravind LA, Pisabarro MT, Seshagiri S, Koonin EV, Dixit VM (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. 6 (4): 961–7. doi:10.1016/S1097-2765(05)00086-9. PMID 11090634.
  15. ^ Yoneda T, Imaizumi K, Maeda M, Yui D, Manabe T, Katayama T, Sato N, Gomi F, Morihara T, Mori Y, Miyoshi K, Hitomi J, Ugawa S, Yamada S, Okabe M, Tohyama M (April 2000). "Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein". J. Biol. Chem. 275 (15): 11114–20. doi:10.1074/jbc.275.15.11114. PMID 10753917.

External links

Further reading