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BCL10 is recruited to sites of DNA damage to facilitate DNA double-strand break repair

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Pages 84-94 | Received 26 Aug 2015, Accepted 12 Nov 2015, Published online: 15 Jan 2016

References

  • Isaacson P, Wright DH. Malignant lymphoma of mucosa-associated lymphoid tissue. A distinctive type of B-cell lymphoma. Cancer 1983; 52:1410-6; PMID:6193858; http://dx.doi.org/10.1002/1097-0142(19831015)52:8%3c1410::AID-CNCR2820520813%3e3.0.CO;2-3
  • Rosebeck S, Rehman AO, Lucas PC, McAllister-Lucas LM. From MALT lymphoma to the CBM signalosome: three decades of discovery. Cell Cycle 2011; 10:2485-96; PMID:21750409; http://dx.doi.org/10.4161/cc.10.15.16923
  • Ruland J, Duncan GS, Elia A, del Barco Barrantes I, Nguyen L, Plyte S, Millar DG, Bouchard D, Wakeham A, Ohashi PS, et al. Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure. Cell 2001; 104:33-42; PMID:11163238; http://dx.doi.org/10.1016/S0092-8674(01)00189-1
  • Rueda D, Gaide O, Ho L, Lewkowicz E, Niedergang F, Hailfinger S, Rebeaud F, Guzzardi M, Conne B, Thelen M, et al. Bcl10 controls TCR- and FcgammaR-induced actin polymerization. J Immunol 2007; 178:4373-84; http://dx.doi.org/10.4049/jimmunol.178.7.4373
  • Xue L, Morris SW, Orihuela C, Tuomanen E, Cui X, Wen R, Wang D. Defective development and function of Bcl10-deficient follicular, marginal zone and B1 B cells. Nat Immunol 2003; 4:857-65; PMID:12910267; http://dx.doi.org/10.1038/ni963
  • Thome M, Charton JE, Pelzer C, Hailfinger S. Antigen receptor signaling to NF-kappaB via CARMA1, BCL10, and MALT1. Cold Spring Harbor perspectives in biology 2010; 2:a003004; PMID:20685844; http://dx.doi.org/10.1101/cshperspect.a003004
  • Israel A. The IKK complex, a central regulator of NF-kappaB activation. Cold Spring Harb Perspect Bio 2010; 2:a000158; PMID:20300203; http://dx.doi.org/10.1101/cshperspect.a000158
  • Jiang C, Lin X. Regulation of NF-kappaB by the CARD proteins. Immunol Rev 2012; 246:141-53; PMID:22435552; http://dx.doi.org/10.1111/j.1600-065X.2012.01110.x
  • Nestle FO, Banchereau J, Hart D. Dendritic cells: On the move from bench to bedside. Nat Med 2001; 7:761-5; PMID:11433329; http://dx.doi.org/10.1038/89863
  • Rehman AO, Wang CY. SDF-1alpha promotes invasion of head and neck squamous cell carcinoma by activating NF-kappaB. J Biol Chem 2008; 283:19888-94; PMID:18448428; http://dx.doi.org/10.1074/jbc.M710432200
  • Jiang T, Grabiner B, Zhu Y, Jiang C, Li H, You Y, Lang J, Hung MC, Lin X. CARMA3 is crucial for EGFR-Induced activation of NF-kappaB and tumor progression. Cancer Res 2011; 71:2183-92; PMID:21406399; http://dx.doi.org/10.1158/0008-5472.CAN-10-3626
  • Ismail IH, Andrin C, McDonald D, Hendzel MJ. BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair. J Cell Biol 2010; 191:45-60; PMID:20921134; http://dx.doi.org/10.1083/jcb.201003034
  • Bennardo N, Cheng A, Huang N, Stark JM. Alternative-NHEJ is a mechanistically distinct pathway of mammalian chromosome break repair. PLoS Gen 2008; 4:e1000110; PMID:18584027; http://dx.doi.org/10.1371/journal.pgen.1000110
  • Dronyk A. New roles for B cell lymphoma 10 in the nucleus. MSc thesis. Edmonton, Alberta, Canada: Alberta, 2011:165.
  • McManus KJ, Hendzel MJ. ATM-dependent DNA damage-independent mitotic phosphorylation of H2AX in normally growing mammalian cells. Mol Biol Cell 2005; 16:5013-25; PMID:16030261; http://dx.doi.org/10.1091/mbc.E05-01-0065
  • Hao LY, Strong MA, Greider CW. Phosphorylation of H2AX at short telomeres in T cells and fibroblasts. J Biol Chem 2004; 279:45148-54; PMID:15322096; http://dx.doi.org/10.1074/jbc.M403924200
  • Lukas C, Savic V, Bekker-Jensen S, Doil C, Neumann B, Pedersen RS, Grofte M, Chan KL, Hickson ID, Bartek J, et al. 53BP1 nuclear bodies form around DNA lesions generated by mitotic transmission of chromosomes under replication stress. Nat Cell Biol 2011; 13:243-53; PMID:21317883; http://dx.doi.org/10.1038/ncb2201
  • Harrigan JA, Belotserkovskaya R, Coates J, Dimitrova DS, Polo SE, Bradshaw CR, Fraser P, Jackson SP. Replication stress induces 53BP1-containing OPT domains in G1 cells. J Cell Biol 2011; 193:97-108; PMID:21444690; http://dx.doi.org/10.1083/jcb.201011083
  • Yuan J, Adamski R, Chen J. Focus on histone variant H2AX: to be or not to be. FEBS Lett 2010; 584:3717-24; PMID:20493860; http://dx.doi.org/10.1016/j.febslet.2010.05.021
  • Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER, 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, et al. ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science 2007; 316:1160-6; PMID:17525332; http://dx.doi.org/10.1126/science.1140321
  • Zeng H, Di L, Fu G, Chen Y, Gao X, Xu L, Lin X, Wen R. Phosphorylation of Bcl10 negatively regulates T-cell receptor-mediated NF-kappaB activation. Mol Cell Biol 2007; 27:5235-45; PMID:17502353; http://dx.doi.org/10.1128/MCB.01645-06
  • Woelk T, Sigismund S, Penengo L, Polo S. The ubiquitination code: a signalling problem. Cell Div 2007; 2:11; PMID:17355622; http://dx.doi.org/10.1186/1747-1028-2-11
  • Nguyen LK, Kolch W, Kholodenko BN. When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling. Cell Commun Signal 2013; 11:52; PMID:23902637; http://dx.doi.org/10.1186/1478-811X-11-52
  • Zhou H, Wertz I, O'Rourke K, Ultsch M, Seshagiri S, Eby M, Xiao W, Dixit VM. Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO. Nature 2004; 427:167-71; PMID:14695475; http://dx.doi.org/10.1038/nature02273
  • Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol Cell 2004; 14:289-301; PMID:15125833; http://dx.doi.org/10.1016/S1097-2765(04)00236-9
  • Powell SN, Kachnic LA. Roles of BRCA1 and BRCA2 in homologous recombination, DNA replication fidelity and the cellular response to ionizing radiation. Oncogene 2003; 22:5784-91; PMID:12947386; http://dx.doi.org/10.1038/sj.onc.1206678
  • Huertas P. DNA resection in eukaryotes: deciding how to fix the break. Nat Struct Mol Biol 2010; 17:11-6; PMID:20051983; http://dx.doi.org/10.1038/nsmb.1710
  • Pommier Y. Topoisomerase I inhibitors: camptothecins and beyond. Nat Rev Cancer 2006; 6:789-802; PMID:16990856; http://dx.doi.org/10.1038/nrc1977
  • Volcic M, Karl S, Baumann B, Salles D, Daniel P, Fulda S, Wiesmuller L. NF-kappaB regulates DNA double-strand break repair in conjunction with BRCA1-CtIP complexes. Nucleic Acids Res 2012; 40:181-95; PMID:21908405; http://dx.doi.org/10.1093/nar/gkr687
  • Doil C, Mailand N, Bekker-Jensen S, Menard P, Larsen DH, Pepperkok R, Ellenberg J, Panier S, Durocher D, Bartek J, et al. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 2009; 136:435-46; PMID:19203579; http://dx.doi.org/10.1016/j.cell.2008.12.041
  • Stewart GS, Panier S, Townsend K, Al-Hakim AK, Kolas NK, Miller ES, Nakada S, Ylanko J, Olivarius S, Mendez M, et al. The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 2009; 136:420-34; PMID:19203578; http://dx.doi.org/10.1016/j.cell.2008.12.042
  • Kolas NK, Chapman JR, Nakada S, Ylanko J, Chahwan R, Sweeney FD, Panier S, Mendez M, Wildenhain J, Thomson TM, et al. Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase. Science 2007; 318:1637-40; PMID:18006705; http://dx.doi.org/10.1126/science.1150034
  • Huen MS, Grant R, Manke I, Minn K, Yu X, Yaffe MB, Chen J. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 2007; 131:901-14; PMID:18001825; http://dx.doi.org/10.1016/j.cell.2007.09.041
  • Mailand N, Bekker-Jensen S, Faustrup H, Melander F, Bartek J, Lukas C, Lukas J. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 2007; 131:887-900; PMID:18001824; http://dx.doi.org/10.1016/j.cell.2007.09.040
  • Zhao H, Zhu M, Dou G, Zhao H, Zhu B, Li J, Liao J, Xu X. BCL10 regulates RNF8/RNF168-mediated ubiquitination in the DNA damage response. Cell cycle 2014; 13:1777-87; PMID:24732096; http://dx.doi.org/10.4161/cc.28707
  • Thome M. CARMA1, BCL-10 and MALT1 in lymphocyte development and activation. Nat Rev Immunol 2004; 4:348-59; PMID:15122200; http://dx.doi.org/10.1038/nri1352

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