The MORC family

References

• Iyer LM, Abhiman S, Aravind L. MutL homologs in restriction-modification systems and the origin of eukaryotic MORC ATPases. Biol Direct 2008; 3:8; http://dx.doi.org/10.1186/1745-6150-3-8; PMID: 18346280
   PubMed Web of Science ®Google Scholar
• Iyer LM, Anantharaman V, Wolf MY, Aravind L. Comparative genomics of transcription factors and chromatin proteins in parasitic protists and other eukaryotes. Int J Parasitol 2008; 38:1 - 31; http://dx.doi.org/10.1016/j.ijpara.2007.07.018; PMID: 17949725
   PubMed Web of Science ®Google Scholar
• Inoue N, Hess KD, Moreadith RW, Richardson LL, Handel MA, Watson ML, et al. New gene family defined by MORC, a nuclear protein required for mouse spermatogenesis. Hum Mol Genet 1999; 8:1201 - 7; http://dx.doi.org/10.1093/hmg/8.7.1201; PMID: 10369865
   PubMed Web of Science ®Google Scholar
• Li DQ, Nair SS, Ohshiro K, Kumar A, Nair VS, Pakala SB, et al. MORC2 signaling integrates phosphorylation-dependent, ATPase-coupled chromatin remodeling during the DNA damage response. Cell Rep 2012; 2:1657 - 69; http://dx.doi.org/10.1016/j.celrep.2012.11.018; PMID: 23260667
   PubMed Web of Science ®Google Scholar
• Kimura Y, Sakai F, Nakano O, Kisaki O, Sugimoto H, Sawamura T, et al. The newly identified human nuclear protein NXP-2 possesses three distinct domains, the nuclear matrix-binding, RNA-binding, and coiled-coil domains. J Biol Chem 2002; 277:20611 - 7; http://dx.doi.org/10.1074/jbc.M201440200; PMID: 11927593
   PubMed Web of Science ®Google Scholar
• Watson ML, Zinn AR, Inoue N, Hess KD, Cobb J, Handel MA, et al. Identification of morc (microrchidia), a mutation that results in arrest of spermatogenesis at an early meiotic stage in the mouse. Proc Natl Acad Sci U S A 1998; 95:14361 - 6; http://dx.doi.org/10.1073/pnas.95.24.14361; PMID: 9826705
   PubMed Web of Science ®Google Scholar
• Condomines M, Hose D, Raynaud P, Hundemer M, De Vos J, Baudard M, et al. Cancer/testis genes in multiple myeloma: expression patterns and prognosis value determined by microarray analysis. J Immunol 2007; 178:3307 - 15; PMID: 17312182
   PubMed Web of Science ®Google Scholar
• Shah SP, Morin RD, Khattra J, Prentice L, Pugh T, Burleigh A, et al. Mutational evolution in a lobular breast tumour profiled at single nucleotide resolution. Nature 2009; 461:809 - 13; http://dx.doi.org/10.1038/nature08489; PMID: 19812674
   PubMed Web of Science ®Google Scholar
• Tripathi A, King C, de la Morenas A, Perry VK, Burke B, Antoine GA, et al. Gene expression abnormalities in histologically normal breast epithelium of breast cancer patients. Int J Cancer 2008; 122:1557 - 66; http://dx.doi.org/10.1002/ijc.23267; PMID: 18058819
   PubMed Web of Science ®Google Scholar
• Chen LH, Kuo WH, Tsai MH, Chen PC, Hsiao CK, Chuang EY, et al. Identification of prognostic genes for recurrent risk prediction in triple negative breast cancer patients in Taiwan. PLoS One 2011; 6:e28222; http://dx.doi.org/10.1371/journal.pone.0028222; PMID: 22140552
   PubMed Web of Science ®Google Scholar
• Takahashi K, Yoshida N, Murakami N, Kawata K, Ishizaki H, Tanaka-Okamoto M, et al. Dynamic regulation of p53 subnuclear localization and senescence by MORC3. Mol Biol Cell 2007; 18:1701 - 9; http://dx.doi.org/10.1091/mbc.E06-08-0747; PMID: 17332504
   PubMed Web of Science ®Google Scholar
• Mimura Y, Takahashi K, Kawata K, Akazawa T, Inoue N. Two-step colocalization of MORC3 with PML nuclear bodies. J Cell Sci 2010; 123:2014 - 24; http://dx.doi.org/10.1242/jcs.063586; PMID: 20501696
   PubMed Web of Science ®Google Scholar
• González-Fernández R, Morales M, Avila J, Martín-Vasallo P. Changes in leukocyte gene expression profiles induced by antineoplastic chemotherapy. Oncol Lett 2012; 3:1341 - 9; PMID: 22783446
   PubMed Web of Science ®Google Scholar
• Liggins AP, Cooper CD, Lawrie CH, Brown PJ, Collins GP, Hatton CS, et al. MORC4, a novel member of the MORC family, is highly expressed in a subset of diffuse large B-cell lymphomas. Br J Haematol 2007; 138:479 - 86; http://dx.doi.org/10.1111/j.1365-2141.2007.06680.x; PMID: 17608765
   PubMed Web of Science ®Google Scholar
• Lemmers RJ, Tawil R, Petek LM, Balog J, Block GJ, Santen GW, et al. Digenic inheritance of an SMCHD1 mutation and an FSHD-permissive D4Z4 allele causes facioscapulohumeral muscular dystrophy type 2. Nat Genet 2012; 44:1370 - 4; http://dx.doi.org/10.1038/ng.2454; PMID: 23143600
   PubMed Web of Science ®Google Scholar
• Shao Y, Li Y, Zhang J, Liu D, Liu F, Zhao Y, et al. Involvement of histone deacetylation in MORC2-mediated down-regulation of carbonic anhydrase IX. Nucleic Acids Res 2010; 38:2813 - 24; http://dx.doi.org/10.1093/nar/gkq006; PMID: 20110259
   PubMed Web of Science ®Google Scholar
• Wang GL, Wang CY, Cai XZ, Chen W, Wang XH, Li F. Identification and expression analysis of a novel CW-type zinc finger protein MORC2 in cancer cells. Anat Rec (Hoboken) 2010; 293:1002 - 9; http://dx.doi.org/10.1002/ar.21119; PMID: 20225202
   PubMedGoogle Scholar
• Bernardi R, Pandolfi PP. Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies. Nat Rev Mol Cell Biol 2007; 8:1006 - 16; http://dx.doi.org/10.1038/nrm2277; PMID: 17928811
   PubMed Web of Science ®Google Scholar
• Draskovic I, Arnoult N, Steiner V, Bacchetti S, Lomonte P, Londoño-Vallejo A. Probing PML body function in ALT cells reveals spatiotemporal requirements for telomere recombination. Proc Natl Acad Sci U S A 2009; 106:15726 - 31; http://dx.doi.org/10.1073/pnas.0907689106; PMID: 19717459
   PubMed Web of Science ®Google Scholar
• Lang M, Jegou T, Chung I, Richter K, Münch S, Udvarhelyi A, et al. Three-dimensional organization of promyelocytic leukemia nuclear bodies. J Cell Sci 2010; 123:392 - 400; http://dx.doi.org/10.1242/jcs.053496; PMID: 20130140
   PubMed Web of Science ®Google Scholar
• Torok D, Ching RW, Bazett-Jones DP. PML nuclear bodies as sites of epigenetic regulation. Front Biosci 2009; 14:1325 - 36; http://dx.doi.org/10.2741/3311; PMID: 19273133
   PubMed Web of Science ®Google Scholar
• Blewitt ME, Gendrel AV, Pang Z, Sparrow DB, Whitelaw N, Craig JM, et al. SmcHD1, containing a structural-maintenance-of-chromosomes hinge domain, has a critical role in X inactivation. Nat Genet 2008; 40:663 - 9; http://dx.doi.org/10.1038/ng.142; PMID: 18425126
   PubMed Web of Science ®Google Scholar
• Losada A, Hirano T. Dynamic molecular linkers of the genome: the first decade of SMC proteins. Genes Dev 2005; 19:1269 - 87; http://dx.doi.org/10.1101/gad.1320505; PMID: 15937217
   PubMed Web of Science ®Google Scholar
• Leong HS, Chen K, Hu Y, Lee S, Corbin J, Pakusch M, et al. Epigenetic regulator Smchd1 functions as a tumor suppressor. Cancer Res 2013; 73:1591 - 9; http://dx.doi.org/10.1158/0008-5472.CAN-12-3019; PMID: 23269277
   PubMed Web of Science ®Google Scholar
• Tirard M, Hsiao HH, Nikolov M, Urlaub H, Melchior F, Brose N. In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice. Proc Natl Acad Sci U S A 2012; 109:21122 - 7; http://dx.doi.org/10.1073/pnas.1215366110; PMID: 23213215
   PubMed Web of Science ®Google Scholar
• Moissiard G, Cokus SJ, Cary J, Feng S, Billi AC, Stroud H, et al. MORC family ATPases required for heterochromatin condensation and gene silencing. Science 2012; 336:1448 - 51; http://dx.doi.org/10.1126/science.1221472; PMID: 22555433
   PubMed Web of Science ®Google Scholar
• Dutta R, Inouye M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem Sci 2000; 25:24 - 8; http://dx.doi.org/10.1016/S0968-0004(99)01503-0; PMID: 10637609
   PubMed Web of Science ®Google Scholar
• Hu X, Machius M, Yang W. Monovalent cation dependence and preference of GHKL ATPases and kinases. FEBS Lett 2003; 544:268 - 73; http://dx.doi.org/10.1016/S0014-5793(03)00519-2; PMID: 12782329
   PubMed Web of Science ®Google Scholar
• Vignali M, Hassan AH, Neely KE, Workman JL. ATP-dependent chromatin-remodeling complexes. Mol Cell Biol 2000; 20:1899 - 910; http://dx.doi.org/10.1128/MCB.20.6.1899-1910.2000; PMID: 10688638
   PubMed Web of Science ®Google Scholar
• Clapier CR, Cairns BR. The biology of chromatin remodeling complexes. Annu Rev Biochem 2009; 78:273 - 304; http://dx.doi.org/10.1146/annurev.biochem.77.062706.153223; PMID: 19355820
   PubMed Web of Science ®Google Scholar
• Meyer P, Prodromou C, Hu B, Vaughan C, Roe SM, Panaretou B, et al. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Mol Cell 2003; 11:647 - 58; http://dx.doi.org/10.1016/S1097-2765(03)00065-0; PMID: 12667448
   PubMed Web of Science ®Google Scholar
• Ban C, Junop M, Yang W. Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell 1999; 97:85 - 97; http://dx.doi.org/10.1016/S0092-8674(00)80717-5; PMID: 10199405
   PubMed Web of Science ®Google Scholar
• Räschle M, Dufner P, Marra G, Jiricny J. Mutations within the hMLH1 and hPMS2 subunits of the human MutLalpha mismatch repair factor affect its ATPase activity, but not its ability to interact with hMutSalpha. J Biol Chem 2002; 277:21810 - 20; http://dx.doi.org/10.1074/jbc.M108787200; PMID: 11948175
   PubMed Web of Science ®Google Scholar
• Corbett KD, Berger JM. Structural dissection of ATP turnover in the prototypical GHL ATPase TopoVI. Structure 2005; 13:873 - 82; http://dx.doi.org/10.1016/j.str.2005.03.013; PMID: 15939019
   PubMed Web of Science ®Google Scholar
• Böhmdorfer G, Schleiffer A, Brunmeir R, Ferscha S, Nizhynska V, Kozák J, et al. GMI1, a structural-maintenance-of-chromosomes-hinge domain-containing protein, is involved in somatic homologous recombination in Arabidopsis. Plant J 2011; 67:420 - 33; http://dx.doi.org/10.1111/j.1365-313X.2011.04604.x; PMID: 21481027
   PubMed Web of Science ®Google Scholar
• Lorković ZJ, Naumann U, Matzke AJ, Matzke M. Involvement of a GHKL ATPase in RNA-directed DNA methylation in Arabidopsis thaliana. Curr Biol 2012; 22:933 - 8; http://dx.doi.org/10.1016/j.cub.2012.03.061; PMID: 22560611
   PubMed Web of Science ®Google Scholar
• He F, Umehara T, Saito K, Harada T, Watanabe S, Yabuki T, et al. Structural insight into the zinc finger CW domain as a histone modification reader. Structure 2010; 18:1127 - 39; http://dx.doi.org/10.1016/j.str.2010.06.012; PMID: 20826339
   PubMed Web of Science ®Google Scholar
• Hoppmann V, Thorstensen T, Kristiansen PE, Veiseth SV, Rahman MA, Finne K, et al. The CW domain, a new histone recognition module in chromatin proteins. EMBO J 2011; 30:1939 - 52; http://dx.doi.org/10.1038/emboj.2011.108; PMID: 21522130
   PubMed Web of Science ®Google Scholar
• Li X, Foley EA, Molloy KR, Li Y, Chait BT, Kapoor TM. Quantitative chemical proteomics approach to identify post-translational modification-mediated protein-protein interactions. J Am Chem Soc 2012; 134:1982 - 5; http://dx.doi.org/10.1021/ja210528v; PMID: 22239320
   PubMed Web of Science ®Google Scholar
• Perry J, Zhao Y. The CW domain, a structural module shared amongst vertebrates, vertebrate-infecting parasites and higher plants. Trends Biochem Sci 2003; 28:576 - 80; http://dx.doi.org/10.1016/j.tibs.2003.09.007; PMID: 14607086
   PubMed Web of Science ®Google Scholar
• Aravind L, Abhiman S, Iyer LM. Natural history of the eukaryotic chromatin protein methylation system. Prog Mol Biol Transl Sci 2011; 101:105 - 76; http://dx.doi.org/10.1016/B978-0-12-387685-0.00004-4; PMID: 21507350
   PubMed Web of Science ®Google Scholar
• Zhao Z, Yu Y, Meyer D, Wu C, Shen WH. Prevention of early flowering by expression of FLOWERING LOCUS C requires methylation of histone H3 K36. Nat Cell Biol 2005; 7:1256 - 60; http://dx.doi.org/10.1038/ncb1329; PMID: 16299497
   PubMed Web of Science ®Google Scholar
• Zhou Y, Tan B, Luo M, Li Y, Liu C, Chen C, et al. HISTONE DEACETYLASE19 interacts with HSL1 and participates in the repression of seed maturation genes in Arabidopsis seedlings. Plant Cell 2013; 25:134 - 48; http://dx.doi.org/10.1105/tpc.112.096313; PMID: 23362207
   PubMed Web of Science ®Google Scholar
• Suzuki M, Wang HH, McCarty DR. Repression of the LEAFY COTYLEDON 1/B3 regulatory network in plant embryo development by VP1/ABSCISIC ACID INSENSITIVE 3-LIKE B3 genes. Plant Physiol 2007; 143:902 - 11; http://dx.doi.org/10.1104/pp.106.092320; PMID: 17158584
   PubMed Web of Science ®Google Scholar
• Zemach A, Grafi G. Methyl-CpG-binding domain proteins in plants: interpreters of DNA methylation. Trends Plant Sci 2007; 12:80 - 5; http://dx.doi.org/10.1016/j.tplants.2006.12.004; PMID: 17208509
   PubMed Web of Science ®Google Scholar
• Ito M, Koike A, Koizumi N, Sano H. Methylated DNA-binding proteins from Arabidopsis. Plant Physiol 2003; 133:1747 - 54; http://dx.doi.org/10.1104/pp.103.026708; PMID: 14605234
   PubMed Web of Science ®Google Scholar
• Karytinos A, Forneris F, Profumo A, Ciossani G, Battaglioli E, Binda C, et al. A novel mammalian flavin-dependent histone demethylase. J Biol Chem 2009; 284:17775 - 82; http://dx.doi.org/10.1074/jbc.M109.003087; PMID: 19407342
   PubMed Web of Science ®Google Scholar
• Ciccone DN, Su H, Hevi S, Gay F, Lei H, Bajko J, et al. KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints. Nature 2009; 461:415 - 8; http://dx.doi.org/10.1038/nature08315; PMID: 19727073
   PubMed Web of Science ®Google Scholar
• Yang Z, Jiang J, Stewart DM, Qi S, Yamane K, Li J, et al. AOF1 is a histone H3K4 demethylase possessing demethylase activity-independent repression function. Cell Res 2010; 20:276 - 87; http://dx.doi.org/10.1038/cr.2010.12; PMID: 20101264
   PubMed Web of Science ®Google Scholar
• Zhang Q, Qi S, Xu M, Yu L, Tao Y, Deng Z, et al. Structure-function analysis reveals a novel mechanism for regulation of histone demethylase LSD2/AOF1/KDM1b. Cell Res 2013; 23:225 - 41; http://dx.doi.org/10.1038/cr.2012.177; PMID: 23266887
   PubMed Web of Science ®Google Scholar
• Cavalli G, Paro R. Chromo-domain proteins: linking chromatin structure to epigenetic regulation. Curr Opin Cell Biol 1998; 10:354 - 60; http://dx.doi.org/10.1016/S0955-0674(98)80011-2; PMID: 9640536
   PubMed Web of Science ®Google Scholar
• Tajul-Arifin K, Teasdale R, Ravasi T, Hume DA, Mattick JS, RIKEN GER Group, GSL Members. Identification and analysis of chromodomain-containing proteins encoded in the mouse transcriptome. Genome Res 2003; 13:6B 1416 - 29; http://dx.doi.org/10.1101/gr.1015703; PMID: 12819141
   PubMed Web of Science ®Google Scholar
• Jones DO, Cowell IG, Singh PB. Mammalian chromodomain proteins: their role in genome organisation and expression. Bioessays 2000; 22:124 - 37; http://dx.doi.org/10.1002/(SICI)1521-1878(200002)22:2<124::AID-BIES4>3.0.CO;2-E; PMID: 10655032
   PubMed Web of Science ®Google Scholar
• Ceol CJ, Houvras Y, Jane-Valbuena J, Bilodeau S, Orlando DA, Battisti V, et al. The histone methyltransferase SETDB1 is recurrently amplified in melanoma and accelerates its onset. Nature 2011; 471:513 - 7; http://dx.doi.org/10.1038/nature09806; PMID: 21430779
   PubMed Web of Science ®Google Scholar
• Mason JM, Arndt KM. Coiled coil domains: stability, specificity, and biological implications. Chembiochem 2004; 5:170 - 6; http://dx.doi.org/10.1002/cbic.200300781; PMID: 14760737
   PubMed Web of Science ®Google Scholar
• McFarlane AA, Orriss GL, Stetefeld J. The use of coiled-coil proteins in drug delivery systems. Eur J Pharmacol 2009; 625:101 - 7; http://dx.doi.org/10.1016/j.ejphar.2009.05.034; PMID: 19835864
   PubMed Web of Science ®Google Scholar
• Lupas AN, Gruber M. The structure of α-helical coiled coils. Adv Protein Chem 2005; 70:37 - 78; http://dx.doi.org/10.1016/S0065-3233(05)70003-6; PMID: 15837513
   PubMedGoogle Scholar
• Li X, He L, Che KH, Funderburk SF, Pan L, Pan N, et al. Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG. Nat Commun 2012; 3:662; http://dx.doi.org/10.1038/ncomms1648; PMID: 22314358
   PubMed Web of Science ®Google Scholar
• Burkhard P, Stetefeld J, Strelkov SV. Coiled coils: a highly versatile protein folding motif. Trends Cell Biol 2001; 11:82 - 8; http://dx.doi.org/10.1016/S0962-8924(00)01898-5; PMID: 11166216
   PubMed Web of Science ®Google Scholar
• Cheng P, Yang Y, Heintzen C, Liu Y. Coiled-coil domain-mediated FRQ-FRQ interaction is essential for its circadian clock function in Neurospora. EMBO J 2001; 20:101 - 8; http://dx.doi.org/10.1093/emboj/20.1.101; PMID: 11226160
   PubMed Web of Science ®Google Scholar
• Peng H, Begg GE, Schultz DC, Friedman JR, Jensen DE, Speicher DW, et al. Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions. J Mol Biol 2000; 295:1139 - 62; http://dx.doi.org/10.1006/jmbi.1999.3402; PMID: 10653693
   PubMed Web of Science ®Google Scholar
• Hurme R, Berndt KD, Namork E, Rhen M. DNA binding exerted by a bacterial gene regulator with an extensive coiled-coil domain. J Biol Chem 1996; 271:12626 - 31; http://dx.doi.org/10.1074/jbc.271.21.12626; PMID: 8647874
   PubMed Web of Science ®Google Scholar
• Nikolay R, Wiederkehr T, Rist W, Kramer G, Mayer MP, Bukau B. Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J Biol Chem 2004; 279:2673 - 8; http://dx.doi.org/10.1074/jbc.M311112200; PMID: 14610072
   PubMed Web of Science ®Google Scholar
• Parachoniak CA, Park M. Distinct recruitment of Eps15 via Its coiled-coil domain is required for efficient down-regulation of the met receptor tyrosine kinase. J Biol Chem 2009; 284:8382 - 94; http://dx.doi.org/10.1074/jbc.M807607200; PMID: 19109251
   PubMed Web of Science ®Google Scholar
• Tanner MJ, Hanel W, Gaffen SL, Lin X. CARMA1 coiled-coil domain is involved in the oligomerization and subcellular localization of CARMA1 and is required for T cell receptor-induced NF-kappaB activation. J Biol Chem 2007; 282:17141 - 7; http://dx.doi.org/10.1074/jbc.M700169200; PMID: 17428801
   PubMed Web of Science ®Google Scholar
• Tao W, Malone CL, Ault AD, Deschenes RJ, Fassler JS. A cytoplasmic coiled-coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1. Mol Microbiol 2002; 43:459 - 73; http://dx.doi.org/10.1046/j.1365-2958.2002.02757.x; PMID: 11985722
   PubMed Web of Science ®Google Scholar
• Fanelli M, Fantozzi A, De Luca P, Caprodossi S, Matsuzawa S, Lazar MA, et al. The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome. J Biol Chem 2004; 279:5374 - 9; http://dx.doi.org/10.1074/jbc.M306407200; PMID: 14645235
   PubMed Web of Science ®Google Scholar
• Yang K, Zhu J, Sun S, Tang Y, Zhang B, Diao L, et al. The coiled-coil domain of TRAF6 is essential for its auto-ubiquitination. Biochem Biophys Res Commun 2004; 324:432 - 9; http://dx.doi.org/10.1016/j.bbrc.2004.09.070; PMID: 15465037
   PubMed Web of Science ®Google Scholar
• Zhang T, Kee WH, Seow KT, Fung W, Cao X. The coiled-coil domain of Stat3 is essential for its SH2 domain-mediated receptor binding and subsequent activation induced by epidermal growth factor and interleukin-6. Mol Cell Biol 2000; 20:7132 - 9; http://dx.doi.org/10.1128/MCB.20.19.7132-7139.2000; PMID: 10982829
   PubMed Web of Science ®Google Scholar
• Ma J, Zhang T, Novotny-Diermayr V, Tan AL, Cao X. A novel sequence in the coiled-coil domain of Stat3 essential for its nuclear translocation. J Biol Chem 2003; 278:29252 - 60; http://dx.doi.org/10.1074/jbc.M304196200; PMID: 12746441
   PubMed Web of Science ®Google Scholar
• Raiborg C, Bremnes B, Mehlum A, Gillooly DJ, D’Arrigo A, Stang E, et al. FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. J Cell Sci 2001; 114:2255 - 63; PMID: 11493665
   PubMed Web of Science ®Google Scholar
• Begitt A, Meyer T, van Rossum M, Vinkemeier U. Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain. Proc Natl Acad Sci U S A 2000; 97:10418 - 23; http://dx.doi.org/10.1073/pnas.190318397; PMID: 10973496
   PubMed Web of Science ®Google Scholar
• Blazek D, Barboric M, Kohoutek J, Oven I, Peterlin BM. Oligomerization of HEXIM1 via 7SK snRNA and coiled-coil region directs the inhibition of P-TEFb. Nucleic Acids Res 2005; 33:7000 - 10; http://dx.doi.org/10.1093/nar/gki997; PMID: 16377779
   PubMed Web of Science ®Google Scholar
• Watanabe M, Yanagi Y, Masuhiro Y, Yano T, Yoshikawa H, Yanagisawa J, et al. A putative tumor suppressor, TSG101, acts as a transcriptional suppressor through its coiled-coil domain. Biochem Biophys Res Commun 1998; 245:900 - 5; http://dx.doi.org/10.1006/bbrc.1998.8547; PMID: 9588212
   PubMed Web of Science ®Google Scholar
• Buisson R, Masson JY. PALB2 self-interaction controls homologous recombination. Nucleic Acids Res 2012; 40:10312 - 23; http://dx.doi.org/10.1093/nar/gks807; PMID: 22941656
   PubMed Web of Science ®Google Scholar
• Hohl M, Kwon Y, Galván SM, Xue X, Tous C, Aguilera A, et al. The Rad50 coiled-coil domain is indispensable for Mre11 complex functions. Nat Struct Mol Biol 2011; 18:1124 - 31; http://dx.doi.org/10.1038/nsmb.2116; PMID: 21892167
   PubMed Web of Science ®Google Scholar
• Itakura E, Sawada I, Matsuura A. Dimerization of the ATRIP protein through the coiled-coil motif and its implication to the maintenance of stalled replication forks. Mol Biol Cell 2005; 16:5551 - 62; http://dx.doi.org/10.1091/mbc.E05-05-0427; PMID: 16176973
   PubMed Web of Science ®Google Scholar
• Ball HL, Cortez D. ATRIP oligomerization is required for ATR-dependent checkpoint signaling. J Biol Chem 2005; 280:31390 - 6; http://dx.doi.org/10.1074/jbc.M504961200; PMID: 16027118
   PubMed Web of Science ®Google Scholar
• Bar M, Sharfman M, Schuster S, Avni A. The coiled-coil domain of EHD2 mediates inhibition of LeEix2 endocytosis and signaling. PLoS One 2009; 4:e7973; http://dx.doi.org/10.1371/journal.pone.0007973; PMID: 19936242
   PubMedGoogle Scholar
• Rairdan GJ, Collier SM, Sacco MA, Baldwin TT, Boettrich T, Moffett P. The coiled-coil and nucleotide binding domains of the Potato Rx disease resistance protein function in pathogen recognition and signaling. Plant Cell 2008; 20:739 - 51; http://dx.doi.org/10.1105/tpc.107.056036; PMID: 18344282
   PubMed Web of Science ®Google Scholar
• He Y, Wertheim JA, Xu L, Miller JP, Karnell FG, Choi JK, et al. The coiled-coil domain and Tyr177 of bcr are required to induce a murine chronic myelogenous leukemia-like disease by bcr/abl. Blood 2002; 99:2957 - 68; http://dx.doi.org/10.1182/blood.V99.8.2957; PMID: 11929787
   PubMed Web of Science ®Google Scholar
• Cheng HY, Schiavone AP, Smithgall TE. A point mutation in the N-terminal coiled-coil domain releases c-Fes tyrosine kinase activity and survival signaling in myeloid leukemia cells. Mol Cell Biol 2001; 21:6170 - 80; http://dx.doi.org/10.1128/MCB.21.18.6170-6180.2001; PMID: 11509660
   PubMed Web of Science ®Google Scholar
• Zhang X, Subrahmanyam R, Wong R, Gross AW, Ren R. The NH(2)-terminal coiled-coil domain and tyrosine 177 play important roles in induction of a myeloproliferative disease in mice by Bcr-Abl. Mol Cell Biol 2001; 21:840 - 53; http://dx.doi.org/10.1128/MCB.21.3.840-853.2001; PMID: 11154271
   PubMed Web of Science ®Google Scholar
• Watson AA, Mahajan P, Mertens HD, Deery MJ, Zhang W, Pham P, et al. The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 2012; 422:3 - 17; http://dx.doi.org/10.1016/j.jmb.2012.04.031; PMID: 22575888
   PubMed Web of Science ®Google Scholar
• Rosendorff A, Sakakibara S, Lu S, Kieff E, Xuan Y, DiBacco A, et al. NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression. Proc Natl Acad Sci U S A 2006; 103:5308 - 13; http://dx.doi.org/10.1073/pnas.0601066103; PMID: 16567619
   PubMed Web of Science ®Google Scholar
• Gendrel AV, Apedaile A, Coker H, Termanis A, Zvetkova I, Godwin J, et al. Smchd1-dependent and -independent pathways determine developmental dynamics of CpG island methylation on the inactive X chromosome. Dev Cell 2012; 23:265 - 79; http://dx.doi.org/10.1016/j.devcel.2012.06.011; PMID: 22841499
   PubMed Web of Science ®Google Scholar
• Kanno T, Bucher E, Daxinger L, Huettel B, Böhmdorfer G, Gregor W, et al. A structural-maintenance-of-chromosomes hinge domain-containing protein is required for RNA-directed DNA methylation. Nat Genet 2008; 40:670 - 5; http://dx.doi.org/10.1038/ng.119; PMID: 18425128
   PubMed Web of Science ®Google Scholar
• Kang HG, Hyong WC, von Einem S, Manosalva P, Ehlers K, Liu PP, et al. CRT1 is a nuclear-translocated MORC endonuclease that participates in multiple levels of plant immunity. Nat Commun 2012; 3:1297; http://dx.doi.org/10.1038/ncomms2279; PMID: 23250427
   PubMed Web of Science ®Google Scholar
• Kang HG, Kuhl JC, Kachroo P, Klessig DF. CRT1, an Arabidopsis ATPase that interacts with diverse resistance proteins and modulates disease resistance to turnip crinkle virus. Cell Host Microbe 2008; 3:48 - 57; http://dx.doi.org/10.1016/j.chom.2007.11.006; PMID: 18191794
   PubMed Web of Science ®Google Scholar
• Roberts AR, Blewitt ME, Youngson NA, Whitelaw E, Chong S. Reduced dosage of the modifiers of epigenetic reprogramming Dnmt1, Dnmt3L, SmcHD1 and Foxo3a has no detectable effect on mouse telomere length in vivo. Chromosoma 2011; 120:377 - 85; http://dx.doi.org/10.1007/s00412-011-0318-9; PMID: 21553025
   PubMed Web of Science ®Google Scholar
• Stiff T, O’Driscoll M, Rief N, Iwabuchi K, Löbrich M, Jeggo PA. ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation. Cancer Res 2004; 64:2390 - 6; http://dx.doi.org/10.1158/0008-5472.CAN-03-3207; PMID: 15059890
   PubMed Web of Science ®Google Scholar
• Ward IM, Chen J. Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress. J Biol Chem 2001; 276:47759 - 62; PMID: 11673449
   PubMed Web of Science ®Google Scholar
• Kinner A, Wu W, Staudt C, Iliakis G. Gamma-H2AX in recognition and signaling of DNA double-strand breaks in the context of chromatin. Nucleic Acids Res 2008; 36:5678 - 94; http://dx.doi.org/10.1093/nar/gkn550; PMID: 18772227
   PubMed Web of Science ®Google Scholar
• Rogakou EP, Pilch DR, Orr AH, Ivanova VS, Bonner WM. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 1998; 273:5858 - 68; http://dx.doi.org/10.1074/jbc.273.10.5858; PMID: 9488723
   PubMed Web of Science ®Google Scholar
• Park JH, Park EJ, Lee HS, Kim SJ, Hur SK, Imbalzano AN, et al. Mammalian SWI/SNF complexes facilitate DNA double-strand break repair by promoting gamma-H2AX induction. EMBO J 2006; 25:3986 - 97; http://dx.doi.org/10.1038/sj.emboj.7601291; PMID: 16932743
   PubMed Web of Science ®Google Scholar
• van Attikum H, Fritsch O, Hohn B, Gasser SM. Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. Cell 2004; 119:777 - 88; http://dx.doi.org/10.1016/j.cell.2004.11.033; PMID: 15607975
   PubMed Web of Science ®Google Scholar
• Morrison AJ, Highland J, Krogan NJ, Arbel-Eden A, Greenblatt JF, Haber JE, et al. INO80 and gamma-H2AX interaction links ATP-dependent chromatin remodeling to DNA damage repair. Cell 2004; 119:767 - 75; http://dx.doi.org/10.1016/j.cell.2004.11.037; PMID: 15607974
   PubMed Web of Science ®Google Scholar
• Xu Y, Ayrapetov MK, Xu C, Gursoy-Yuzugullu O, Hu Y, Price BD. Histone H2A.Z controls a critical chromatin remodeling step required for DNA double-strand break repair. Mol Cell 2012; 48:723 - 33; http://dx.doi.org/10.1016/j.molcel.2012.09.026; PMID: 23122415
   PubMed Web of Science ®Google Scholar
• Papamichos-Chronakis M, Watanabe S, Rando OJ, Peterson CL. Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity. Cell 2011; 144:200 - 13; http://dx.doi.org/10.1016/j.cell.2010.12.021; PMID: 21241891
   PubMed Web of Science ®Google Scholar
• Mizuguchi G, Shen X, Landry J, Wu WH, Sen S, Wu C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 2004; 303:343 - 8; http://dx.doi.org/10.1126/science.1090701; PMID: 14645854
   PubMed Web of Science ®Google Scholar
• Morillo-Huesca M, Clemente-Ruiz M, Andújar E, Prado F. The SWR1 histone replacement complex causes genetic instability and genome-wide transcription misregulation in the absence of H2A.Z. PLoS One 2010; 5:e12143; http://dx.doi.org/10.1371/journal.pone.0012143; PMID: 20711347
   PubMed Web of Science ®Google Scholar
• Dellaire G, Ching RW, Ahmed K, Jalali F, Tse KC, Bristow RG, et al. Promyelocytic leukemia nuclear bodies behave as DNA damage sensors whose response to DNA double-strand breaks is regulated by NBS1 and the kinases ATM, Chk2, and ATR. J Cell Biol 2006; 175:55 - 66; http://dx.doi.org/10.1083/jcb.200604009; PMID: 17030982
   PubMed Web of Science ®Google Scholar