PAXX Is an Accessory c-NHEJ Factor that Associates with Ku70 and Has Overlapping Functions with XLF

In mammalian cells, classical non-homologous end joining (c-NHEJ) is critical for DNA double-strand break repair induced by ionizing radiation and during V(D)J recombination in developing B and T lymphocytes. Recently, PAXX was identified as a c-NHEJ core component. We report here that PAXX-deficien...

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Vydáno v:	Cell reports (Cambridge) Ročník 17; číslo 2; s. 541 - 555
Hlavní autoři:	Tadi, Satish K., Tellier-Lebègue, Carine, Nemoz, Clément, Drevet, Pascal, Audebert, Stéphane, Roy, Sunetra, Meek, Katheryn, Charbonnier, Jean-Baptiste, Modesti, Mauro
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Elsevier Inc 04.10.2016 Elsevier
Témata:	B-Lymphocytes - metabolism DNA Breaks, Double-Stranded DNA double-strand break repair DNA End-Joining Repair - genetics DNA ligase 4 DNA Repair - genetics DNA Repair Enzymes - genetics DNA Repair Enzymes - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism HCT116 Cells Humans Ku Autoantigen - chemistry Ku Autoantigen - genetics Ku Autoantigen - metabolism Ku70 Life Sciences MMEJ NHEJ PAXX T-Lymphocytes - metabolism V(D)J recombination V(D)J Recombination - genetics XLF XRCC4 Ku70 DNA double-strand break repair MMEJ XLF PAXX XRCC4 V(D)J recombination DNA ligase 4 Ku NHEJ
ISSN:	2211-1247, 2211-1247
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Abstract	In mammalian cells, classical non-homologous end joining (c-NHEJ) is critical for DNA double-strand break repair induced by ionizing radiation and during V(D)J recombination in developing B and T lymphocytes. Recently, PAXX was identified as a c-NHEJ core component. We report here that PAXX-deficient cells exhibit a cellular phenotype uncharacteristic of a deficiency in c-NHEJ core components. PAXX-deficient cells display normal sensitivity to radiomimetic drugs, are proficient in transient V(D)J recombination assays, and do not shift toward higher micro-homology usage in plasmid repair assays. Although PAXX-deficient cells lack c-NHEJ phenotypes, PAXX forms a stable ternary complex with Ku bound to DNA. Formation of this complex involves an interaction with Ku70 and requires a bare DNA extension for stability. Moreover, the relatively weak Ku-dependent stimulation of LIG4/XRCC4 activity by PAXX is unmasked by XLF ablation. Thus, PAXX plays an accessory role during c-NHEJ that is largely overlapped by XLF’s function. [Display omitted] •PAXX interaction with Ku threaded onto DNA requires a bare DNA extension•PAXX interacts with the Ku70 subunit•PAXX is dispensable for V(D)J recombination and has no core c-NHEJ phenotype•PAXX’s function in c-NHEJ is masked by XLF Tadi et al. find that PAXX interacts with Ku threaded on DNA via the Ku70 subunit and requires a bare DNA extension for stability. They show that PAXX’s function overlaps with c-NHEJ factor XLF, explaining why its ablation has only a mild effect on NHEJ.
AbstractList	In mammalian cells, classical non-homologous end joining (c-NHEJ) is critical for DNA double-strand break repair induced by ionizing radiation and during V(D)J recombination in developing B and T lymphocytes. Recently, PAXX was identified as a c-NHEJ core component. We report here that PAXX-deficient cells exhibit a cellular phenotype uncharacteristic of a deficiency in c-NHEJ core components. PAXX-deficient cells display normal sensitivity to radiomimetic drugs, are proficient in transient V(D)J recombination assays, and do not shift toward higher micro-homology usage in plasmid repair assays. Although PAXX-deficient cells lack c-NHEJ phenotypes, PAXX forms a stable ternary complex with Ku bound to DNA. Formation of this complex involves an interaction with Ku70 and requires a bare DNA extension for stability. Moreover, the relatively weak Ku-dependent stimulation of LIG4/XRCC4 activity by PAXX is unmasked by XLF ablation. Thus, PAXX plays an accessory role during c-NHEJ that is largely overlapped by XLF's function. In mammalian cells, classical non-homologous end joining (c-NHEJ) is critical for DNA double-strand break repair induced by ionizing radiation and during V(D)J recombination in developing B and T lymphocytes. Recently, PAXX was identified as a c-NHEJ core component. We report here that PAXX-deficient cells exhibit a cellular phenotype uncharacteristic of a deficiency in c-NHEJ core components. PAXX-deficient cells display normal sensitivity to radiomimetic drugs, are proficient in transient V(D)J recombination assays, and do not shift toward higher micro-homology usage in plasmid repair assays. Although PAXX-deficient cells lack c-NHEJ phenotypes, PAXX forms a stable ternary complex with Ku bound to DNA. Formation of this complex involves an interaction with Ku70 and requires a bare DNA extension for stability. Moreover, the relatively weak Ku-dependent stimulation of LIG4/XRCC4 activity by PAXX is unmasked by XLF ablation. Thus, PAXX plays an accessory role during c-NHEJ that is largely overlapped by XLF’s function. [Display omitted] •PAXX interaction with Ku threaded onto DNA requires a bare DNA extension•PAXX interacts with the Ku70 subunit•PAXX is dispensable for V(D)J recombination and has no core c-NHEJ phenotype•PAXX’s function in c-NHEJ is masked by XLF Tadi et al. find that PAXX interacts with Ku threaded on DNA via the Ku70 subunit and requires a bare DNA extension for stability. They show that PAXX’s function overlaps with c-NHEJ factor XLF, explaining why its ablation has only a mild effect on NHEJ. In mammalian cells, classical non-homologous end joining (c-NHEJ) is critical for DNA double-strand break repair induced by ionizing radiation and during V(D)J recombination in developing B and T lymphocytes. Recently, PAXX was identified as a c-NHEJ core component. We report here that PAXX-deficient cells exhibit a cellular phenotype uncharacteristic of a deficiency in c-NHEJ core components. PAXX-deficient cells display normal sensitivity to radiomimetic drugs, are proficient in transient V(D)J recombination assays, and do not shift toward higher micro-homology usage in plasmid repair assays. Although PAXX-deficient cells lack c-NHEJ phenotypes, PAXX forms a stable ternary complex with Ku bound to DNA. Formation of this complex involves an interaction with Ku70 and requires a bare DNA extension for stability. Moreover, the relatively weak Ku-dependent stimulation of LIG4/XRCC4 activity by PAXX is unmasked by XLF ablation. Thus, PAXX plays an accessory role during c-NHEJ that is largely overlapped by XLF's function.
Author	Roy, Sunetra Nemoz, Clément Drevet, Pascal Audebert, Stéphane Tellier-Lebègue, Carine Charbonnier, Jean-Baptiste Tadi, Satish K. Modesti, Mauro Meek, Katheryn
Author_xml	– sequence: 1 givenname: Satish K. surname: Tadi fullname: Tadi, Satish K. organization: Cancer Research Center of Marseille, CNRS UMR7258, INSERM U1068, Institut Paoli-Calmettes, Aix-Marseille Université UM105, 13273 Marseille, France – sequence: 2 givenname: Carine surname: Tellier-Lebègue fullname: Tellier-Lebègue, Carine organization: Institute for Integrative Biology of the Cell (I2BC), IBITECS, CEA, CNRS, University Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France – sequence: 3 givenname: Clément surname: Nemoz fullname: Nemoz, Clément organization: Institute for Integrative Biology of the Cell (I2BC), IBITECS, CEA, CNRS, University Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France – sequence: 4 givenname: Pascal surname: Drevet fullname: Drevet, Pascal organization: Institute for Integrative Biology of the Cell (I2BC), IBITECS, CEA, CNRS, University Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France – sequence: 5 givenname: Stéphane surname: Audebert fullname: Audebert, Stéphane organization: Cancer Research Center of Marseille, CNRS UMR7258, INSERM U1068, Institut Paoli-Calmettes, Aix-Marseille Université UM105, 13273 Marseille, France – sequence: 6 givenname: Sunetra surname: Roy fullname: Roy, Sunetra organization: Department of Microbiology & Molecular Genetics, and Department of Pathobiology & Diagnostic Investigation, College of Veterinary Medicine, Michigan State University, East Lansing, MI 48824, USA – sequence: 7 givenname: Katheryn surname: Meek fullname: Meek, Katheryn organization: Department of Microbiology & Molecular Genetics, and Department of Pathobiology & Diagnostic Investigation, College of Veterinary Medicine, Michigan State University, East Lansing, MI 48824, USA – sequence: 8 givenname: Jean-Baptiste surname: Charbonnier fullname: Charbonnier, Jean-Baptiste organization: Institute for Integrative Biology of the Cell (I2BC), IBITECS, CEA, CNRS, University Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette cedex, France – sequence: 9 givenname: Mauro surname: Modesti fullname: Modesti, Mauro email: mauro.modesti@inserm.fr organization: Cancer Research Center of Marseille, CNRS UMR7258, INSERM U1068, Institut Paoli-Calmettes, Aix-Marseille Université UM105, 13273 Marseille, France
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Cites_doi	10.1093/nar/gkr656 10.1016/j.dnarep.2013.12.006 10.1016/j.dnarep.2014.02.007 10.1016/j.molcel.2007.10.024 10.1016/0022-2836(67)90307-5 10.1101/cshperspect.a012757 10.1016/S1568-7864(02)00235-5 10.1038/nature09604 10.1016/S0065-2776(04)86002-4 10.1002/1521-4141(200203)32:3<701::AID-IMMU701>3.0.CO;2-T 10.1093/nar/22.19.3918 10.1146/annurev-genet-110711-155540 10.1667/0033-7587(2003)160[0291:AOTDPK]2.0.CO;2 10.1038/emboj.2012.304 10.1016/j.dnarep.2014.02.011 10.1093/bmb/ldv020 10.1038/ncomms11242 10.1016/j.dnarep.2014.02.008 10.1006/prep.1998.1003 10.1093/nar/gkq387 10.1093/nar/gkr1211 10.1158/0008-5472.CAN-04-3055 10.1128/MCB.01503-14 10.1074/jbc.274.28.20034 10.1073/pnas.0702620104 10.1093/nar/gkn957 10.1038/35088000 10.1084/jem.186.6.921 10.1074/jbc.273.2.842 10.1074/jbc.M112.440388 10.1146/annurev.biochem.052308.093131 10.1126/science.1261971 10.1016/j.cell.2007.10.005 10.1038/ncomms7233 10.1016/j.pep.2006.10.002 10.1093/nar/gkm579 10.1038/nature08926 10.1002/em.21725 10.1016/0006-291X(90)92385-D 10.4049/jimmunol.1501654 10.1128/MCB.01895-08 10.1093/nar/gks1326 10.1038/cdd.2015.22 10.1093/nar/27.24.4679 10.1016/j.molcel.2015.01.005 10.1093/emboj/18.7.2008 10.1038/nprot.2013.143 10.1016/j.jmb.2005.11.028 10.1016/0014-5793(94)00863-9 10.1016/j.dnarep.2014.04.015 10.1093/nar/gkv1145 10.1093/nar/gkp283 10.1074/jbc.273.47.31068
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Keywords	Ku70 DNA double-strand break repair MMEJ XLF PAXX XRCC4 V(D)J recombination DNA ligase 4 Ku NHEJ
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References	Walker, Corpina, Goldberg (bib42) 2001; 412 Audebert, Salles, Weinfeld, Calsou (bib4) 2006; 356 Akopiants, Zhou, Mohapatra, Valerie, Lees-Miller, Lee, Chen, Revy, de Villartay, Povirk (bib1) 2009; 37 Nussenzweig, Nussenzweig (bib26) 2007; 131 Ono, Tucker, Capra (bib30) 1994; 22 Frit, Barboule, Yuan, Gomez, Calsou (bib13) 2014; 17 Shirodkar, Fenton, Meng, Koch (bib38) 2013; 288 Tsai, Kim, Chu (bib39) 2007; 104 Andres, Modesti, Tsai, Chu, Junop (bib3) 2007; 28 Waters, Strande, Wyatt, Pryor, Ramsden (bib47) 2014; 17 Zha, Guo, Boboila, Oksenych, Cheng, Zhang, Wesemann, Yuen, Patel, Goff (bib53) 2011; 469 Deriano, Roth (bib9) 2013; 47 Fattah, Kweon, Wang, Lee, Kan, Lichter, Weisensel, Hendrickson (bib12) 2014; 15 Grundy, Rulten, Zeng, Arribas-Bosacoma, Iles, Manley, Oliver, Caldecott (bib14) 2013; 32 Wang, Rosidi, Perrault, Wang, Zhang, Windhofer, Iliakis (bib46) 2005; 65 Dudley, Chaudhuri, Bassing, Alt (bib10) 2005; 86 Woodbine, Gennery, Jeggo (bib48) 2014; 16 Craxton, Somers, Munnur, Jukes-Jones, Cain, Malewicz (bib7) 2015; 22 Riballo, Woodbine, Stiff, Walker, Goodarzi, Jeggo (bib34) 2009; 37 Yoo, Kimzey, Dynan (bib52) 1999; 274 Sheffield, Garrard, Derewenda (bib37) 1999; 15 Allaway, Vivino, Kohn, Notkins, Prabhakar (bib2) 1990; 168 Wang, Satoh, Chou, Reeves (bib43) 1994; 351 Xing, Yang, Huo, Feng, Wei, Jiang, Ning, Yan, Li, Wang (bib50) 2015; 6 Vizcaíno, Csordas, del-Toro, Dianes, Griss, Lavidas, Mayer, Perez-Riverol, Reisinger, Ternent (bib41) 2016; 44 Roberts, Strande, Burkhalter, Strom, Havener, Hasty, Ramsden (bib35) 2010; 464 Ouyang, Nussenzweig, Kurimasa, Soares, Li, Cordon-Cardo, Li, Cheong, Nussenzweig, Iliakis (bib31) 1997; 186 Modesti, Hesse, Gellert (bib24) 1999; 18 Liu, Gan, Guo, Xie, Gao, Guo, Zhang, Willis, Su, Asara (bib20) 2015; 57 Cheng, Barboule, Frit, Gomez, Bombarde, Couderc, Ren, Salles, Calsou (bib5) 2011; 39 Elmroth, Nygren, Mårtensson, Ismail, Hammarsten (bib11) 2003; 2 Oh, Harvey, Zimbric, Wang, Nguyen, Jackson, Hendrickson (bib29) 2014; 21 Mårtensson, Nygren, Osheroff, Hammarsten (bib22) 2003; 160 Grundy, Rulten, Arribas-Bosacoma, Davidson, Kozik, Oliver, Pearl, Caldecott (bib15) 2016; 7 Roy, de Melo, Xu, Tadi, Négrel, Hendrickson, Modesti, Meek (bib36) 2015; 35 Oh, Wang, Zimbric, Hendrickson (bib28) 2013; 41 Yoo, Dynan (bib51) 1999; 27 Ran, Hsu, Wright, Agarwala, Scott, Zhang (bib33) 2013; 8 Mansour, Rhein, Dahm-Daphi (bib21) 2010; 38 Neal, Xu, Abe, Hendrickson, Meek (bib25) 2016; 196 Verkaik, Esveldt-van Lange, van Heemst, Brüggenwirth, Hoeijmakers, Zdzienicka, van Gent (bib40) 2002; 32 Hanakahi (bib17) 2007; 52 Lieber (bib19) 2010; 79 Wang, Dong, Myung, Hendrickson, Reeves (bib44) 1998; 273 Hirt (bib18) 1967; 26 de Villartay (bib8) 2015; 114 Ochi, Blackford, Coates, Jhujh, Mehmood, Tamura, Travers, Wu, Draviam, Robinson (bib27) 2015; 347 Wang, Dong, Reeves (bib45) 1998; 273 Ramsden, Asagoshi (bib32) 2012; 53 Wu, Frit, Meesala, Dauvillier, Modesti, Andres, Huang, Sekiguchi, Calsou, Salles, Junop (bib49) 2009; 29 Gu, Lu, Tsai, Schwarz, Lieber (bib16) 2007; 35 Chiruvella, Liang, Wilson (bib6) 2013; 5 Meek, Lees-Miller, Modesti (bib23) 2012; 40 Craxton (10.1016/j.celrep.2016.09.026_bib7) 2015; 22 de Villartay (10.1016/j.celrep.2016.09.026_bib8) 2015; 114 Hanakahi (10.1016/j.celrep.2016.09.026_bib17) 2007; 52 Tsai (10.1016/j.celrep.2016.09.026_bib39) 2007; 104 Andres (10.1016/j.celrep.2016.09.026_bib3) 2007; 28 Ochi (10.1016/j.celrep.2016.09.026_bib27) 2015; 347 Shirodkar (10.1016/j.celrep.2016.09.026_bib38) 2013; 288 Verkaik (10.1016/j.celrep.2016.09.026_bib40) 2002; 32 Waters (10.1016/j.celrep.2016.09.026_bib47) 2014; 17 Deriano (10.1016/j.celrep.2016.09.026_bib9) 2013; 47 Grundy (10.1016/j.celrep.2016.09.026_bib14) 2013; 32 Gu (10.1016/j.celrep.2016.09.026_bib16) 2007; 35 Ono (10.1016/j.celrep.2016.09.026_bib30) 1994; 22 Lieber (10.1016/j.celrep.2016.09.026_bib19) 2010; 79 Akopiants (10.1016/j.celrep.2016.09.026_bib1) 2009; 37 Nussenzweig (10.1016/j.celrep.2016.09.026_bib26) 2007; 131 Ouyang (10.1016/j.celrep.2016.09.026_bib31) 1997; 186 Roy (10.1016/j.celrep.2016.09.026_bib36) 2015; 35 Riballo (10.1016/j.celrep.2016.09.026_bib34) 2009; 37 Allaway (10.1016/j.celrep.2016.09.026_bib2) 1990; 168 Elmroth (10.1016/j.celrep.2016.09.026_bib11) 2003; 2 Ramsden (10.1016/j.celrep.2016.09.026_bib32) 2012; 53 Wang (10.1016/j.celrep.2016.09.026_bib45) 1998; 273 Wang (10.1016/j.celrep.2016.09.026_bib43) 1994; 351 Meek (10.1016/j.celrep.2016.09.026_bib23) 2012; 40 Wang (10.1016/j.celrep.2016.09.026_bib46) 2005; 65 Frit (10.1016/j.celrep.2016.09.026_bib13) 2014; 17 Oh (10.1016/j.celrep.2016.09.026_bib28) 2013; 41 Audebert (10.1016/j.celrep.2016.09.026_bib4) 2006; 356 Dudley (10.1016/j.celrep.2016.09.026_bib10) 2005; 86 Oh (10.1016/j.celrep.2016.09.026_bib29) 2014; 21 Liu (10.1016/j.celrep.2016.09.026_bib20) 2015; 57 Fattah (10.1016/j.celrep.2016.09.026_bib12) 2014; 15 Hirt (10.1016/j.celrep.2016.09.026_bib18) 1967; 26 Roberts (10.1016/j.celrep.2016.09.026_bib35) 2010; 464 Woodbine (10.1016/j.celrep.2016.09.026_bib48) 2014; 16 Wang (10.1016/j.celrep.2016.09.026_bib44) 1998; 273 Zha (10.1016/j.celrep.2016.09.026_bib53) 2011; 469 Ran (10.1016/j.celrep.2016.09.026_bib33) 2013; 8 Sheffield (10.1016/j.celrep.2016.09.026_bib37) 1999; 15 Mansour (10.1016/j.celrep.2016.09.026_bib21) 2010; 38 Modesti (10.1016/j.celrep.2016.09.026_bib24) 1999; 18 Wu (10.1016/j.celrep.2016.09.026_bib49) 2009; 29 Grundy (10.1016/j.celrep.2016.09.026_bib15) 2016; 7 Vizcaíno (10.1016/j.celrep.2016.09.026_bib41) 2016; 44 Yoo (10.1016/j.celrep.2016.09.026_bib51) 1999; 27 Walker (10.1016/j.celrep.2016.09.026_bib42) 2001; 412 Mårtensson (10.1016/j.celrep.2016.09.026_bib22) 2003; 160 Chiruvella (10.1016/j.celrep.2016.09.026_bib6) 2013; 5 Neal (10.1016/j.celrep.2016.09.026_bib25) 2016; 196 Xing (10.1016/j.celrep.2016.09.026_bib50) 2015; 6 Cheng (10.1016/j.celrep.2016.09.026_bib5) 2011; 39 Yoo (10.1016/j.celrep.2016.09.026_bib52) 1999; 274
References_xml	– volume: 38 start-page: 6065 year: 2010 end-page: 6077 ident: bib21 article-title: The alternative end-joining pathway for repair of DNA double-strand breaks requires PARP1 but is not dependent upon microhomologies publication-title: Nucleic Acids Res. – volume: 15 start-page: 39 year: 2014 end-page: 53 ident: bib12 article-title: A role for XLF in DNA repair and recombination in human somatic cells publication-title: DNA Repair (Amst.) – volume: 16 start-page: 84 year: 2014 end-page: 96 ident: bib48 article-title: The clinical impact of deficiency in DNA non-homologous end-joining publication-title: DNA Repair (Amst.) – volume: 168 start-page: 747 year: 1990 end-page: 755 ident: bib2 article-title: Characterization of the 70KDA component of the human Ku autoantigen expressed in insect cell nuclei using a recombinant baculovirus vector publication-title: Biochem. Biophys. Res. Commun. – volume: 274 start-page: 20034 year: 1999 end-page: 20039 ident: bib52 article-title: Photocross-linking of an oriented DNA repair complex. Ku bound at a single DNA end publication-title: J. Biol. Chem. – volume: 186 start-page: 921 year: 1997 end-page: 929 ident: bib31 article-title: Ku70 is required for DNA repair but not for T cell antigen receptor gene recombination In vivo publication-title: J. Exp. Med. – volume: 35 start-page: 3017 year: 2015 end-page: 3028 ident: bib36 article-title: XRCC4/XLF interaction is variably required for DNA repair and is not required for ligase IV stimulation publication-title: Mol. Cell. Biol. – volume: 464 start-page: 1214 year: 2010 end-page: 1217 ident: bib35 article-title: Ku is a 5′-dRP/AP lyase that excises nucleotide damage near broken ends publication-title: Nature – volume: 18 start-page: 2008 year: 1999 end-page: 2018 ident: bib24 article-title: DNA binding of Xrcc4 protein is associated with V(D)J recombination but not with stimulation of DNA ligase IV activity publication-title: EMBO J. – volume: 41 start-page: 1734 year: 2013 end-page: 1749 ident: bib28 article-title: Human LIGIV is synthetically lethal with the loss of Rad54B-dependent recombination and is required for certain chromosome fusion events induced by telomere dysfunction publication-title: Nucleic Acids Res. – volume: 104 start-page: 7851 year: 2007 end-page: 7856 ident: bib39 article-title: Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA ends publication-title: Proc. Natl. Acad. Sci. USA – volume: 53 start-page: 741 year: 2012 end-page: 751 ident: bib32 article-title: DNA polymerases in nonhomologous end joining: are there any benefits to standing out from the crowd? publication-title: Environ. Mol. Mutagen. – volume: 196 start-page: 3032 year: 2016 end-page: 3042 ident: bib25 article-title: Restoration of ATM expression in DNA-PKcs-deficient cells inhibits signal end joining publication-title: J. Immunol. – volume: 65 start-page: 4020 year: 2005 end-page: 4030 ident: bib46 article-title: DNA ligase III as a candidate component of backup pathways of nonhomologous end joining publication-title: Cancer Res. – volume: 37 start-page: 482 year: 2009 end-page: 492 ident: bib34 article-title: XLF-Cernunnos promotes DNA ligase IV-XRCC4 re-adenylation following ligation publication-title: Nucleic Acids Res. – volume: 27 start-page: 4679 year: 1999 end-page: 4686 ident: bib51 article-title: Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein publication-title: Nucleic Acids Res. – volume: 29 start-page: 3163 year: 2009 end-page: 3172 ident: bib49 article-title: Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4 publication-title: Mol. Cell. Biol. – volume: 273 start-page: 842 year: 1998 end-page: 848 ident: bib44 article-title: Identification of two domains of the p70 Ku protein mediating dimerization with p80 and DNA binding publication-title: J. Biol. Chem. – volume: 6 start-page: 6233 year: 2015 ident: bib50 article-title: Interactome analysis identifies a new paralogue of XRCC4 in non-homologous end joining DNA repair pathway publication-title: Nat. Commun. – volume: 273 start-page: 31068 year: 1998 end-page: 31074 ident: bib45 article-title: A model for Ku heterodimer assembly and interaction with DNA. Implications for the function of Ku antigen publication-title: J. Biol. Chem. – volume: 5 start-page: a012757 year: 2013 ident: bib6 article-title: Repair of double-strand breaks by end joining publication-title: Cold Spring Harb. Perspect. Biol. – volume: 15 start-page: 34 year: 1999 end-page: 39 ident: bib37 article-title: Overcoming expression and purification problems of RhoGDI using a family of “parallel” expression vectors publication-title: Protein Expr. Purif. – volume: 28 start-page: 1093 year: 2007 end-page: 1101 ident: bib3 article-title: Crystal structure of human XLF: a twist in nonhomologous DNA end-joining publication-title: Mol. Cell – volume: 469 start-page: 250 year: 2011 end-page: 254 ident: bib53 article-title: ATM damage response and XLF repair factor are functionally redundant in joining DNA breaks publication-title: Nature – volume: 114 start-page: 157 year: 2015 end-page: 167 ident: bib8 article-title: Congenital defects in V(D)J recombination publication-title: Br. Med. Bull. – volume: 351 start-page: 219 year: 1994 end-page: 224 ident: bib43 article-title: Similar DNA binding properties of free P70 (KU) subunit and P70/P80 heterodimer publication-title: FEBS Lett. – volume: 8 start-page: 2281 year: 2013 end-page: 2308 ident: bib33 article-title: Genome engineering using the CRISPR-Cas9 system publication-title: Nat. Protoc. – volume: 57 start-page: 648 year: 2015 end-page: 661 ident: bib20 article-title: Akt-mediated phosphorylation of XLF impairs non-homologous end-joining DNA repair publication-title: Mol. Cell – volume: 26 start-page: 365 year: 1967 end-page: 369 ident: bib18 article-title: Selective extraction of polyoma DNA from infected mouse cell cultures publication-title: J. Mol. Biol. – volume: 288 start-page: 19604 year: 2013 end-page: 19613 ident: bib38 article-title: Identification and functional characterization of a Ku-binding motif in aprataxin polynucleotide kinase/phosphatase-like factor (APLF) publication-title: J. Biol. Chem. – volume: 17 start-page: 81 year: 2014 end-page: 97 ident: bib13 article-title: Alternative end-joining pathway(s): bricolage at DNA breaks publication-title: DNA Repair (Amst.) – volume: 40 start-page: 2964 year: 2012 end-page: 2973 ident: bib23 article-title: N-terminal constraint activates the catalytic subunit of the DNA-dependent protein kinase in the absence of DNA or Ku publication-title: Nucleic Acids Res. – volume: 347 start-page: 185 year: 2015 end-page: 188 ident: bib27 article-title: DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair publication-title: Science – volume: 47 start-page: 433 year: 2013 end-page: 455 ident: bib9 article-title: Modernizing the nonhomologous end-joining repertoire: alternative and classical NHEJ share the stage publication-title: Annu. Rev. Genet. – volume: 44 start-page: D447 year: 2016 end-page: D456 ident: bib41 article-title: 2016 update of the PRIDE database and its related tools publication-title: Nucleic Acids Res. – volume: 160 start-page: 291 year: 2003 end-page: 301 ident: bib22 article-title: Activation of the DNA-dependent protein kinase by drug-induced and radiation-induced DNA strand breaks publication-title: Radiat. Res. – volume: 21 start-page: 97 year: 2014 end-page: 110 ident: bib29 article-title: DNA ligase III and DNA ligase IV carry out genetically distinct forms of end joining in human somatic cells publication-title: DNA Repair (Amst.) – volume: 356 start-page: 257 year: 2006 end-page: 265 ident: bib4 article-title: Involvement of polynucleotide kinase in a poly(ADP-ribose) polymerase-1-dependent DNA double-strand breaks rejoining pathway publication-title: J. Mol. Biol. – volume: 2 start-page: 363 year: 2003 end-page: 374 ident: bib11 article-title: Cleavage of cellular DNA by calicheamicin gamma1 publication-title: DNA Repair (Amst.) – volume: 412 start-page: 607 year: 2001 end-page: 614 ident: bib42 article-title: Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair publication-title: Nature – volume: 7 start-page: 11242 year: 2016 ident: bib15 article-title: The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins publication-title: Nat. Commun. – volume: 52 start-page: 139 year: 2007 end-page: 145 ident: bib17 article-title: 2-Step purification of the Ku DNA repair protein expressed in Escherichia coli publication-title: Protein Expr. Purif. – volume: 131 start-page: 223 year: 2007 end-page: 225 ident: bib26 article-title: A backup DNA repair pathway moves to the forefront publication-title: Cell – volume: 32 start-page: 701 year: 2002 end-page: 709 ident: bib40 article-title: Different types of V(D)J recombination and end-joining defects in DNA double-strand break repair mutant mammalian cells publication-title: Eur. J. Immunol. – volume: 22 start-page: 3918 year: 1994 end-page: 3924 ident: bib30 article-title: Production and characterization of recombinant human Ku antigen publication-title: Nucleic Acids Res. – volume: 37 start-page: 4055 year: 2009 end-page: 4062 ident: bib1 article-title: Requirement for XLF/Cernunnos in alignment-based gap filling by DNA polymerases lambda and mu for nonhomologous end joining in human whole-cell extracts publication-title: Nucleic Acids Res. – volume: 86 start-page: 43 year: 2005 end-page: 112 ident: bib10 article-title: Mechanism and control of V(D)J recombination versus class switch recombination: similarities and differences publication-title: Adv. Immunol. – volume: 22 start-page: 890 year: 2015 end-page: 897 ident: bib7 article-title: XLS (c9orf142) is a new component of mammalian DNA double-stranded break repair publication-title: Cell Death Differ. – volume: 35 start-page: 5755 year: 2007 end-page: 5762 ident: bib16 article-title: Single-stranded DNA ligation and XLF-stimulated incompatible DNA end ligation by the XRCC4-DNA ligase IV complex: influence of terminal DNA sequence publication-title: Nucleic Acids Res. – volume: 17 start-page: 39 year: 2014 end-page: 51 ident: bib47 article-title: Nonhomologous end joining: a good solution for bad ends publication-title: DNA Repair (Amst.) – volume: 79 start-page: 181 year: 2010 end-page: 211 ident: bib19 article-title: The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway publication-title: Annu. Rev. Biochem. – volume: 32 start-page: 112 year: 2013 end-page: 125 ident: bib14 article-title: APLF promotes the assembly and activity of non-homologous end joining protein complexes publication-title: EMBO J. – volume: 39 start-page: 9605 year: 2011 end-page: 9619 ident: bib5 article-title: Ku counteracts mobilization of PARP1 and MRN in chromatin damaged with DNA double-strand breaks publication-title: Nucleic Acids Res. – volume: 39 start-page: 9605 year: 2011 ident: 10.1016/j.celrep.2016.09.026_bib5 article-title: Ku counteracts mobilization of PARP1 and MRN in chromatin damaged with DNA double-strand breaks publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkr656 – volume: 15 start-page: 39 year: 2014 ident: 10.1016/j.celrep.2016.09.026_bib12 article-title: A role for XLF in DNA repair and recombination in human somatic cells publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2013.12.006 – volume: 17 start-page: 81 year: 2014 ident: 10.1016/j.celrep.2016.09.026_bib13 article-title: Alternative end-joining pathway(s): bricolage at DNA breaks publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2014.02.007 – volume: 28 start-page: 1093 year: 2007 ident: 10.1016/j.celrep.2016.09.026_bib3 article-title: Crystal structure of human XLF: a twist in nonhomologous DNA end-joining publication-title: Mol. Cell doi: 10.1016/j.molcel.2007.10.024 – volume: 26 start-page: 365 year: 1967 ident: 10.1016/j.celrep.2016.09.026_bib18 article-title: Selective extraction of polyoma DNA from infected mouse cell cultures publication-title: J. Mol. Biol. doi: 10.1016/0022-2836(67)90307-5 – volume: 5 start-page: a012757 year: 2013 ident: 10.1016/j.celrep.2016.09.026_bib6 article-title: Repair of double-strand breaks by end joining publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a012757 – volume: 2 start-page: 363 year: 2003 ident: 10.1016/j.celrep.2016.09.026_bib11 article-title: Cleavage of cellular DNA by calicheamicin gamma1 publication-title: DNA Repair (Amst.) doi: 10.1016/S1568-7864(02)00235-5 – volume: 469 start-page: 250 year: 2011 ident: 10.1016/j.celrep.2016.09.026_bib53 article-title: ATM damage response and XLF repair factor are functionally redundant in joining DNA breaks publication-title: Nature doi: 10.1038/nature09604 – volume: 86 start-page: 43 year: 2005 ident: 10.1016/j.celrep.2016.09.026_bib10 article-title: Mechanism and control of V(D)J recombination versus class switch recombination: similarities and differences publication-title: Adv. Immunol. doi: 10.1016/S0065-2776(04)86002-4 – volume: 32 start-page: 701 year: 2002 ident: 10.1016/j.celrep.2016.09.026_bib40 article-title: Different types of V(D)J recombination and end-joining defects in DNA double-strand break repair mutant mammalian cells publication-title: Eur. J. Immunol. doi: 10.1002/1521-4141(200203)32:3<701::AID-IMMU701>3.0.CO;2-T – volume: 22 start-page: 3918 year: 1994 ident: 10.1016/j.celrep.2016.09.026_bib30 article-title: Production and characterization of recombinant human Ku antigen publication-title: Nucleic Acids Res. doi: 10.1093/nar/22.19.3918 – volume: 47 start-page: 433 year: 2013 ident: 10.1016/j.celrep.2016.09.026_bib9 article-title: Modernizing the nonhomologous end-joining repertoire: alternative and classical NHEJ share the stage publication-title: Annu. Rev. Genet. doi: 10.1146/annurev-genet-110711-155540 – volume: 160 start-page: 291 year: 2003 ident: 10.1016/j.celrep.2016.09.026_bib22 article-title: Activation of the DNA-dependent protein kinase by drug-induced and radiation-induced DNA strand breaks publication-title: Radiat. Res. doi: 10.1667/0033-7587(2003)160[0291:AOTDPK]2.0.CO;2 – volume: 32 start-page: 112 year: 2013 ident: 10.1016/j.celrep.2016.09.026_bib14 article-title: APLF promotes the assembly and activity of non-homologous end joining protein complexes publication-title: EMBO J. doi: 10.1038/emboj.2012.304 – volume: 16 start-page: 84 year: 2014 ident: 10.1016/j.celrep.2016.09.026_bib48 article-title: The clinical impact of deficiency in DNA non-homologous end-joining publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2014.02.011 – volume: 114 start-page: 157 year: 2015 ident: 10.1016/j.celrep.2016.09.026_bib8 article-title: Congenital defects in V(D)J recombination publication-title: Br. Med. Bull. doi: 10.1093/bmb/ldv020 – volume: 7 start-page: 11242 year: 2016 ident: 10.1016/j.celrep.2016.09.026_bib15 article-title: The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins publication-title: Nat. Commun. doi: 10.1038/ncomms11242 – volume: 17 start-page: 39 year: 2014 ident: 10.1016/j.celrep.2016.09.026_bib47 article-title: Nonhomologous end joining: a good solution for bad ends publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2014.02.008 – volume: 15 start-page: 34 year: 1999 ident: 10.1016/j.celrep.2016.09.026_bib37 article-title: Overcoming expression and purification problems of RhoGDI using a family of “parallel” expression vectors publication-title: Protein Expr. Purif. doi: 10.1006/prep.1998.1003 – volume: 38 start-page: 6065 year: 2010 ident: 10.1016/j.celrep.2016.09.026_bib21 article-title: The alternative end-joining pathway for repair of DNA double-strand breaks requires PARP1 but is not dependent upon microhomologies publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq387 – volume: 40 start-page: 2964 year: 2012 ident: 10.1016/j.celrep.2016.09.026_bib23 article-title: N-terminal constraint activates the catalytic subunit of the DNA-dependent protein kinase in the absence of DNA or Ku publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkr1211 – volume: 65 start-page: 4020 year: 2005 ident: 10.1016/j.celrep.2016.09.026_bib46 article-title: DNA ligase III as a candidate component of backup pathways of nonhomologous end joining publication-title: Cancer Res. doi: 10.1158/0008-5472.CAN-04-3055 – volume: 35 start-page: 3017 year: 2015 ident: 10.1016/j.celrep.2016.09.026_bib36 article-title: XRCC4/XLF interaction is variably required for DNA repair and is not required for ligase IV stimulation publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.01503-14 – volume: 274 start-page: 20034 year: 1999 ident: 10.1016/j.celrep.2016.09.026_bib52 article-title: Photocross-linking of an oriented DNA repair complex. Ku bound at a single DNA end publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.28.20034 – volume: 104 start-page: 7851 year: 2007 ident: 10.1016/j.celrep.2016.09.026_bib39 article-title: Cernunnos/XLF promotes the ligation of mismatched and noncohesive DNA ends publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0702620104 – volume: 37 start-page: 482 year: 2009 ident: 10.1016/j.celrep.2016.09.026_bib34 article-title: XLF-Cernunnos promotes DNA ligase IV-XRCC4 re-adenylation following ligation publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkn957 – volume: 412 start-page: 607 year: 2001 ident: 10.1016/j.celrep.2016.09.026_bib42 article-title: Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair publication-title: Nature doi: 10.1038/35088000 – volume: 186 start-page: 921 year: 1997 ident: 10.1016/j.celrep.2016.09.026_bib31 article-title: Ku70 is required for DNA repair but not for T cell antigen receptor gene recombination In vivo publication-title: J. Exp. Med. doi: 10.1084/jem.186.6.921 – volume: 273 start-page: 842 year: 1998 ident: 10.1016/j.celrep.2016.09.026_bib44 article-title: Identification of two domains of the p70 Ku protein mediating dimerization with p80 and DNA binding publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.2.842 – volume: 288 start-page: 19604 year: 2013 ident: 10.1016/j.celrep.2016.09.026_bib38 article-title: Identification and functional characterization of a Ku-binding motif in aprataxin polynucleotide kinase/phosphatase-like factor (APLF) publication-title: J. Biol. Chem. doi: 10.1074/jbc.M112.440388 – volume: 79 start-page: 181 year: 2010 ident: 10.1016/j.celrep.2016.09.026_bib19 article-title: The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.052308.093131 – volume: 347 start-page: 185 year: 2015 ident: 10.1016/j.celrep.2016.09.026_bib27 article-title: DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair publication-title: Science doi: 10.1126/science.1261971 – volume: 131 start-page: 223 year: 2007 ident: 10.1016/j.celrep.2016.09.026_bib26 article-title: A backup DNA repair pathway moves to the forefront publication-title: Cell doi: 10.1016/j.cell.2007.10.005 – volume: 6 start-page: 6233 year: 2015 ident: 10.1016/j.celrep.2016.09.026_bib50 article-title: Interactome analysis identifies a new paralogue of XRCC4 in non-homologous end joining DNA repair pathway publication-title: Nat. Commun. doi: 10.1038/ncomms7233 – volume: 52 start-page: 139 year: 2007 ident: 10.1016/j.celrep.2016.09.026_bib17 article-title: 2-Step purification of the Ku DNA repair protein expressed in Escherichia coli publication-title: Protein Expr. Purif. doi: 10.1016/j.pep.2006.10.002 – volume: 35 start-page: 5755 year: 2007 ident: 10.1016/j.celrep.2016.09.026_bib16 article-title: Single-stranded DNA ligation and XLF-stimulated incompatible DNA end ligation by the XRCC4-DNA ligase IV complex: influence of terminal DNA sequence publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkm579 – volume: 464 start-page: 1214 year: 2010 ident: 10.1016/j.celrep.2016.09.026_bib35 article-title: Ku is a 5′-dRP/AP lyase that excises nucleotide damage near broken ends publication-title: Nature doi: 10.1038/nature08926 – volume: 53 start-page: 741 year: 2012 ident: 10.1016/j.celrep.2016.09.026_bib32 article-title: DNA polymerases in nonhomologous end joining: are there any benefits to standing out from the crowd? publication-title: Environ. Mol. Mutagen. doi: 10.1002/em.21725 – volume: 168 start-page: 747 year: 1990 ident: 10.1016/j.celrep.2016.09.026_bib2 article-title: Characterization of the 70KDA component of the human Ku autoantigen expressed in insect cell nuclei using a recombinant baculovirus vector publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(90)92385-D – volume: 196 start-page: 3032 year: 2016 ident: 10.1016/j.celrep.2016.09.026_bib25 article-title: Restoration of ATM expression in DNA-PKcs-deficient cells inhibits signal end joining publication-title: J. Immunol. doi: 10.4049/jimmunol.1501654 – volume: 29 start-page: 3163 year: 2009 ident: 10.1016/j.celrep.2016.09.026_bib49 article-title: Structural and functional interaction between the human DNA repair proteins DNA ligase IV and XRCC4 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.01895-08 – volume: 41 start-page: 1734 year: 2013 ident: 10.1016/j.celrep.2016.09.026_bib28 article-title: Human LIGIV is synthetically lethal with the loss of Rad54B-dependent recombination and is required for certain chromosome fusion events induced by telomere dysfunction publication-title: Nucleic Acids Res. doi: 10.1093/nar/gks1326 – volume: 22 start-page: 890 year: 2015 ident: 10.1016/j.celrep.2016.09.026_bib7 article-title: XLS (c9orf142) is a new component of mammalian DNA double-stranded break repair publication-title: Cell Death Differ. doi: 10.1038/cdd.2015.22 – volume: 27 start-page: 4679 year: 1999 ident: 10.1016/j.celrep.2016.09.026_bib51 article-title: Geometry of a complex formed by double strand break repair proteins at a single DNA end: recruitment of DNA-PKcs induces inward translocation of Ku protein publication-title: Nucleic Acids Res. doi: 10.1093/nar/27.24.4679 – volume: 57 start-page: 648 year: 2015 ident: 10.1016/j.celrep.2016.09.026_bib20 article-title: Akt-mediated phosphorylation of XLF impairs non-homologous end-joining DNA repair publication-title: Mol. Cell doi: 10.1016/j.molcel.2015.01.005 – volume: 18 start-page: 2008 year: 1999 ident: 10.1016/j.celrep.2016.09.026_bib24 article-title: DNA binding of Xrcc4 protein is associated with V(D)J recombination but not with stimulation of DNA ligase IV activity publication-title: EMBO J. doi: 10.1093/emboj/18.7.2008 – volume: 8 start-page: 2281 year: 2013 ident: 10.1016/j.celrep.2016.09.026_bib33 article-title: Genome engineering using the CRISPR-Cas9 system publication-title: Nat. Protoc. doi: 10.1038/nprot.2013.143 – volume: 356 start-page: 257 year: 2006 ident: 10.1016/j.celrep.2016.09.026_bib4 article-title: Involvement of polynucleotide kinase in a poly(ADP-ribose) polymerase-1-dependent DNA double-strand breaks rejoining pathway publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.11.028 – volume: 351 start-page: 219 year: 1994 ident: 10.1016/j.celrep.2016.09.026_bib43 article-title: Similar DNA binding properties of free P70 (KU) subunit and P70/P80 heterodimer publication-title: FEBS Lett. doi: 10.1016/0014-5793(94)00863-9 – volume: 21 start-page: 97 year: 2014 ident: 10.1016/j.celrep.2016.09.026_bib29 article-title: DNA ligase III and DNA ligase IV carry out genetically distinct forms of end joining in human somatic cells publication-title: DNA Repair (Amst.) doi: 10.1016/j.dnarep.2014.04.015 – volume: 44 start-page: D447 issue: D1 year: 2016 ident: 10.1016/j.celrep.2016.09.026_bib41 article-title: 2016 update of the PRIDE database and its related tools publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkv1145 – volume: 37 start-page: 4055 year: 2009 ident: 10.1016/j.celrep.2016.09.026_bib1 article-title: Requirement for XLF/Cernunnos in alignment-based gap filling by DNA polymerases lambda and mu for nonhomologous end joining in human whole-cell extracts publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkp283 – volume: 273 start-page: 31068 year: 1998 ident: 10.1016/j.celrep.2016.09.026_bib45 article-title: A model for Ku heterodimer assembly and interaction with DNA. Implications for the function of Ku antigen publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.47.31068
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Snippet	In mammalian cells, classical non-homologous end joining (c-NHEJ) is critical for DNA double-strand break repair induced by ionizing radiation and during V(D)J...
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SubjectTerms	B-Lymphocytes - metabolism DNA Breaks, Double-Stranded DNA double-strand break repair DNA End-Joining Repair - genetics DNA ligase 4 DNA Repair - genetics DNA Repair Enzymes - genetics DNA Repair Enzymes - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism HCT116 Cells Humans Ku Autoantigen - chemistry Ku Autoantigen - genetics Ku Autoantigen - metabolism Ku70 Life Sciences MMEJ NHEJ PAXX T-Lymphocytes - metabolism V(D)J recombination V(D)J Recombination - genetics XLF XRCC4
Title	PAXX Is an Accessory c-NHEJ Factor that Associates with Ku70 and Has Overlapping Functions with XLF
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