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Volumn 203, Issue 3, 2013, Pages 457-470

The histone demethylase LSD1/KDM1A promotes the DNA damage response

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEMETHYLASE; PROTEIN KDM1A; PROTEIN LSD1; PROTEIN RNF168; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84890134037     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201302092     Document Type: Article
Times cited : (107)

References (70)
  • 1
    • 82955233157 scopus 로고    scopus 로고
    • The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
    • Acs, K., M.S. Luijsterburg, L. Ackermann, F.A. Salomons, T. Hoppe, and N.P. Dantuma. 2011. The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18:1345-1350. http://dx.doi.org/10.1038/nsmb.2188
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1345-1350
    • Acs, K.1    Luijsterburg, M.S.2    Ackermann, L.3    Salomons, F.A.4    Hoppe, T.5    Dantuma, N.P.6
  • 2
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: who, what, and why
    • Bedford, M.T., and S.G. Clarke. 2009. Protein arginine methylation in mammals: who, what, and why. Mol. Cell. 33:1-13. http://dx.doi.org/10.1016/j.molcel.2008.12.013
    • (2009) Mol. Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 3
    • 34447551681 scopus 로고    scopus 로고
    • Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair
    • Berkovich, E., R.J. Monnat Jr., and M.B. Kastan. 2007. Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair. Nat. Cell Biol. 9:683-690. http://dx.doi.org/10.1038/ncb1599
    • (2007) Nat. Cell Biol , vol.9 , pp. 683-690
    • Berkovich, E.1    Monnat Jr., R.J.2    Kastan, M.B.3
  • 4
    • 43149118801 scopus 로고    scopus 로고
    • Assessment of protein dynamics and DNA repair following generation of DNA double-strand breaks at defined genomic sites
    • Berkovich, E., R.J. Monnat Jr., and M.B. Kastan. 2008. Assessment of protein dynamics and DNA repair following generation of DNA double-strand breaks at defined genomic sites. Nat. Protoc. 3:915-922. http://dx.doi.org/10.1038/nprot.2008.54
    • (2008) Nat. Protoc , vol.3 , pp. 915-922
    • Berkovich, E.1    Monnat Jr., R.J.2    Kastan, M.B.3
  • 5
    • 79955627875 scopus 로고    scopus 로고
    • Genomic instability, defective spermatogenesis, immunodeficiency, and cancer in a mouse model of the RIDDLE syndrome
    • Bohgaki, T., M. Bohgaki, R. Cardoso, S. Panier, D. Zeegers, L. Li, G.S. Stewart, O. Sanchez, M.P. Hande, D. Durocher, et al. 2011. Genomic instability, defective spermatogenesis, immunodeficiency, and cancer in a mouse model of the RIDDLE syndrome. PLoS Genet. 7:e1001381. http://dx.doi.org/10.1371/journal.pgen.1001381
    • (2011) PLoS Genet , vol.7
    • Bohgaki, T.1    Bohgaki, M.2    Cardoso, R.3    Panier, S.4    Zeegers, D.5    Li, L.6    Stewart, G.S.7    Sanchez, O.8    Hande, M.P.9    Durocher, D.10
  • 6
    • 58749092121 scopus 로고    scopus 로고
    • Histone H3 lysine 4 trimethylation marks meiotic recombination initiation sites
    • Borde, V., N. Robine, W. Lin, S. Bonfils, V. Géli, and A. Nicolas. 2009. Histone H3 lysine 4 trimethylation marks meiotic recombination initiation sites. EMBO J. 28:99-111. http://dx.doi.org/10.1038/emboj.2008.257
    • (2009) EMBO J , vol.28 , pp. 99-111
    • Borde, V.1    Robine, N.2    Lin, W.3    Bonfils, S.4    Géli, V.5    Nicolas, A.6
  • 9
    • 76749123506 scopus 로고    scopus 로고
    • Genetics. Genetic control of hotspots
    • Cheung, V.G., S.L. Sherman, and E. Feingold. 2010. Genetics. Genetic control of hotspots. Science. 327:791-792. http://dx.doi.org/10.1126/science.1187155
    • (2010) Science , vol.327 , pp. 791-792
    • Cheung, V.G.1    Sherman, S.L.2    Feingold, E.3
  • 10
    • 79952314830 scopus 로고    scopus 로고
    • Double-strand breaks in heterochromatin move outside of a dynamic HP1a domain to complete recombinational repair
    • Chiolo, I., A. Minoda, S.U. Colmenares, A. Polyzos, S.V. Costes, and G.H. Karpen. 2011. Double-strand breaks in heterochromatin move outside of a dynamic HP1a domain to complete recombinational repair. Cell. 144:732-744. http://dx.doi.org/10.1016/j.cell.2011.02.012
    • (2011) Cell , vol.144 , pp. 732-744
    • Chiolo, I.1    Minoda, A.2    Colmenares, S.U.3    Polyzos, A.4    Costes, S.V.5    Karpen, G.H.6
  • 11
    • 78649349810 scopus 로고    scopus 로고
    • A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage
    • Chou, D.M., B. Adamson, N.E. Dephoure, X. Tan, A.C. Nottke, K.E. Hurov, S.P. Gygi, M.P. Colaiácovo, and S.J. Elledge. 2010. A chromatin localization screen reveals poly (ADP ribose)-regulated recruitment of the repressive polycomb and NuRD complexes to sites of DNA damage. Proc. Natl. Acad. Sci. USA. 107:18475-18480. http://dx.doi.org/10.1073/pnas.1012946107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18475-18480
    • Chou, D.M.1    Adamson, B.2    Dephoure, N.E.3    Tan, X.4    Nottke, A.C.5    Hurov, K.E.6    Gygi, S.P.7    Colaiácovo, M.P.8    Elledge, S.J.9
  • 12
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: making it safe to play with knives
    • Ciccia, A., and S.J. Elledge. 2010. The DNA damage response: making it safe to play with knives. Mol. Cell. 40:179-204. http://dx.doi.org/10.1016/j.molcel.2010.09.019
    • (2010) Mol. Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 13
    • 43249102851 scopus 로고    scopus 로고
    • Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease
    • Cloos, P.A., J. Christensen, K. Agger, and K. Helin. 2008. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. Genes Dev. 22:1115-1140. http://dx.doi.org/10.1101/gad.1652908
    • (2008) Genes Dev , vol.22 , pp. 1115-1140
    • Cloos, P.A.1    Christensen, J.2    Agger, K.3    Helin, K.4
  • 14
    • 77957684964 scopus 로고    scopus 로고
    • The cellular response to DNA damage: a focus on MDC1 and its interacting proteins
    • Coster, G., and M. Goldberg. 2010. The cellular response to DNA damage: a focus on MDC1 and its interacting proteins. Nucleus. 1:166-178. http://dx.doi.org/10.4161/nucl.1.2.11176
    • (2010) Nucleus , vol.1 , pp. 166-178
    • Coster, G.1    Goldberg, M.2
  • 15
    • 80555127349 scopus 로고    scopus 로고
    • DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation
    • Dango, S., N. Mosammaparast, M.E. Sowa, L.J. Xiong, F. Wu, K. Park, M. Rubin, S. Gygi, J.W. Harper, and Y. Shi. 2011. DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA alkylation repair and cancer cell proliferation. Mol. Cell. 44:373-384. http://dx.doi.org/10.1016/j.molcel.2011.08.039
    • (2011) Mol. Cell , vol.44 , pp. 373-384
    • Dango, S.1    Mosammaparast, N.2    Sowa, M.E.3    Xiong, L.J.4    Wu, F.5    Park, K.6    Rubin, M.7    Gygi, S.8    Harper, J.W.9    Shi, Y.10
  • 16
    • 84861915893 scopus 로고    scopus 로고
    • Roles for histone H3K4 methyltransferase activities during immunoglobulin class-switch recombination
    • Daniel, J.A., and A. Nussenzweig. 2012. Roles for histone H3K4 methyltransferase activities during immunoglobulin class-switch recombination. Biochim. Biophys. Acta. 1819:733-738. http://dx.doi.org/10.1016/j.bbagrm.2012.01.019
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 733-738
    • Daniel, J.A.1    Nussenzweig, A.2
  • 17
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
    • Doil, C., N. Mailand, S. Bekker-Jensen, P. Menard, D.H. Larsen, R. Pepperkok, J. Ellenberg, S. Panier, D. Durocher, J. Bartek, et al. 2009. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell. 136:435-446. http://dx.doi.org/10.1016/j.cell.2008.12.041
    • (2009) Cell , vol.136 , pp. 435-446
    • Doil, C.1    Mailand, N.2    Bekker-Jensen, S.3    Menard, P.4    Larsen, D.H.5    Pepperkok, R.6    Ellenberg, J.7    Panier, S.8    Durocher, D.9    Bartek, J.10
  • 18
    • 70349308060 scopus 로고    scopus 로고
    • 53BP1: function and mechanisms of focal recruitment
    • FitzGerald, J.E., M. Grenon, and N.F. Lowndes. 2009. 53BP1: function and mechanisms of focal recruitment. Biochem. Soc. Trans. 37:897-904. http://dx.doi.org/10.1042/BST0370897
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 897-904
    • FitzGerald, J.E.1    Grenon, M.2    Lowndes, N.F.3
  • 21
    • 84863793933 scopus 로고    scopus 로고
    • A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
    • Gatti, M., S. Pinato, E. Maspero, P. Soffientini, S. Polo, and L. Penengo. 2012. A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase. Cell Cycle. 11:2538-2544. http://dx.doi.org/10.4161/cc.20919
    • (2012) Cell Cycle , vol.11 , pp. 2538-2544
    • Gatti, M.1    Pinato, S.2    Maspero, E.3    Soffientini, P.4    Polo, S.5    Penengo, L.6
  • 23
    • 0037188526 scopus 로고    scopus 로고
    • A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes
    • Hakimi, M.A., D.A. Bochar, J. Chenoweth, W.S. Lane, G. Mandel, and R. Shiekhattar. 2002. A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes. Proc. Natl. Acad. Sci. USA. 99:7420-7425. http://dx.doi.org/10.1073/pnas.112008599
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7420-7425
    • Hakimi, M.A.1    Bochar, D.A.2    Chenoweth, J.3    Lane, W.S.4    Mandel, G.5    Shiekhattar, R.6
  • 24
    • 0037470142 scopus 로고    scopus 로고
    • A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes
    • Hakimi, M.A., Y. Dong, W.S. Lane, D.W. Speicher, and R. Shiekhattar. 2003. A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes. J. Biol. Chem. 278:7234-7239. http://dx.doi.org/10.1074/jbc. M208992200
    • (2003) J. Biol. Chem , vol.278 , pp. 7234-7239
    • Hakimi, M.A.1    Dong, Y.2    Lane, W.S.3    Speicher, D.W.4    Shiekhattar, R.5
  • 26
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen, M.S., R. Grant, I. Manke, K. Minn, X. Yu, M.B. Yaffe, and J. Chen. 2007. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell. 131:901-914. http://dx.doi.org/10.1016/j.cell.2007.09.041
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1    Grant, R.2    Manke, I.3    Minn, K.4    Yu, X.5    Yaffe, M.B.6    Chen, J.7
  • 27
    • 75149189204 scopus 로고    scopus 로고
    • BRCA1 and its toolbox for the maintenance of genome integrity
    • Huen, M.S., S.M. Sy, and J. Chen. 2010. BRCA1 and its toolbox for the maintenance of genome integrity. Nat. Rev. Mol. Cell Biol. 11:138-148. http://dx.doi.org/10.1038/nrm2831
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 138-148
    • Huen, M.S.1    Sy, S.M.2    Chen, J.3
  • 28
    • 77957748289 scopus 로고    scopus 로고
    • BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair
    • Ismail, I.H., C. Andrin, D. McDonald, and M.J. Hendzel. 2010. BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair. J. Cell Biol. 191:45-60. http://dx.doi.org/10.1083/jcb.201003034
    • (2010) J. Cell Biol , vol.191 , pp. 45-60
    • Ismail, I.H.1    Andrin, C.2    McDonald, D.3    Hendzel, M.J.4
  • 29
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • Jackson, S.P., and J. Bartek. 2009. The DNA-damage response in human biology and disease. Nature. 461:1071-1078. http://dx.doi.org/10.1038/nature08467
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 30
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose, R.J., and Y. Zhang. 2007. Regulation of histone methylation by demethylimination and demethylation. Nat. Rev. Mol. Cell Biol. 8:307-318. http://dx.doi.org/10.1038/nrm2143
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 33
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • Lee, M.G., C. Wynder, N. Cooch, and R. Shiekhattar. 2005. An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature. 437:432-435.
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 35
    • 77952011032 scopus 로고    scopus 로고
    • LSD1 is required for chromosome segregation during mitosis
    • Lv, S., W. Bu, H. Jiao, B. Liu, L. Zhu, H. Zhao, J. Liao, J. Li, and X. Xu. 2010. LSD1 is required for chromosome segregation during mitosis. Eur. J. Cell Biol. 89:557-563. http://dx.doi.org/10.1016/j.ejcb.2010.01.004
    • (2010) Eur. J. Cell Biol , vol.89 , pp. 557-563
    • Lv, S.1    Bu, W.2    Jiao, H.3    Liu, B.4    Zhu, L.5    Zhao, H.6    Liao, J.7    Li, J.8    Xu, X.9
  • 36
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand, N., S. Bekker-Jensen, H. Faustrup, F. Melander, J. Bartek, C. Lukas, and J. Lukas. 2007. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell. 131:887-900. http://dx.doi.org/10.1016/j.cell.2007.09.040
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3    Melander, F.4    Bartek, J.5    Lukas, C.6    Lukas, J.7
  • 37
    • 84859895529 scopus 로고    scopus 로고
    • RNF8-and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites
    • Mallette, F.A., F. Mattiroli, G. Cui, L.C. Young, M.J. Hendzel, G. Mer, T.K. Sixma, and S. Richard. 2012. RNF8-and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J. 31:1865-1878. http://dx.doi.org/10.1038/emboj.2012.47
    • (2012) EMBO J , vol.31 , pp. 1865-1878
    • Mallette, F.A.1    Mattiroli, F.2    Cui, G.3    Young, L.C.4    Hendzel, M.J.5    Mer, G.6    Sixma, T.K.7    Richard, S.8
  • 41
    • 77956341931 scopus 로고    scopus 로고
    • Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
    • Miller, K.M., J.V. Tjeertes, J. Coates, G. Legube, S.E. Polo, S. Britton, and S.P. Jackson. 2010. Human HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining. Nat. Struct. Mol. Biol. 17:1144-1151. http://dx.doi.org/10.1038/nsmb.1899
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 1144-1151
    • Miller, K.M.1    Tjeertes, J.V.2    Coates, J.3    Legube, G.4    Polo, S.E.5    Britton, S.6    Jackson, S.P.7
  • 42
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast, N., and Y. Shi. 2010. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu. Rev. Biochem. 79:155-179. http://dx.doi.org/10.1146/annurev.biochem.78.070907.103946
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 43
    • 57049167675 scopus 로고    scopus 로고
    • CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation
    • Mulligan, P., T.F. Westbrook, M. Ottinger, N. Pavlova, B. Chang, E. Macia, Y.J. Shi, J. Barretina, J. Liu, P.M. Howley, et al. 2008. CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation. Mol. Cell. 32:718-726. http://dx.doi.org/10.1016/j.molcel.2008.10.025
    • (2008) Mol. Cell , vol.32 , pp. 718-726
    • Mulligan, P.1    Westbrook, T.F.2    Ottinger, M.3    Pavlova, N.4    Chang, B.5    Macia, E.6    Shi, Y.J.7    Barretina, J.8    Liu, J.9    Howley, P.M.10
  • 44
    • 30344444484 scopus 로고    scopus 로고
    • Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
    • Murr, R., J.I. Loizou, Y.G. Yang, C. Cuenin, H. Li, Z.Q. Wang, and Z. Herceg. 2006. Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks. Nat. Cell Biol. 8:91-99. http://dx.doi.org/10.1038/ncb1343
    • (2006) Nat. Cell Biol , vol.8 , pp. 91-99
    • Murr, R.1    Loizou, J.I.2    Yang, Y.G.3    Cuenin, C.4    Li, H.5    Wang, Z.Q.6    Herceg, Z.7
  • 45
    • 0347381286 scopus 로고    scopus 로고
    • Immunoaffinity purification of mammalian protein complexes
    • Nakatani, Y., and V. Ogryzko. 2003. Immunoaffinity purification of mammalian protein complexes. Methods Enzymol. 370:430-444. http://dx.doi.org/10.1016/S0076-6879(03)70037-8
    • (2003) Methods Enzymol , vol.370 , pp. 430-444
    • Nakatani, Y.1    Ogryzko, V.2
  • 47
    • 77956870690 scopus 로고    scopus 로고
    • Regulation of DNA-damage responses and cell-cycle progression by the chromatin remodelling factor CHD4
    • Polo, S.E., A. Kaidi, L. Baskcomb, Y. Galanty, and S.P. Jackson. 2010. Regulation of DNA-damage responses and cell-cycle progression by the chromatin remodelling factor CHD4. EMBO J. 29:3130-3139. http://dx.doi.org/10.1038/emboj.2010.188
    • (2010) EMBO J , vol.29 , pp. 3130-3139
    • Polo, S.E.1    Kaidi, A.2    Baskcomb, L.3    Galanty, Y.4    Jackson, S.P.5
  • 49
    • 34447519212 scopus 로고    scopus 로고
    • The lysine-specific demethylase 1 is required for cell proliferation in both p53-dependent and-independent manners
    • Scoumanne, A., and X. Chen. 2007. The lysine-specific demethylase 1 is required for cell proliferation in both p53-dependent and-independent manners. J. Biol. Chem. 282:15471-15475. http://dx.doi.org/10.1074/jbc. M701023200
    • (2007) J. Biol. Chem , vol.282 , pp. 15471-15475
    • Scoumanne, A.1    Chen, X.2
  • 50
    • 77953720192 scopus 로고    scopus 로고
    • ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks
    • Shanbhag, N.M., I.U. Rafalska-Metcalf, C. Balane-Bolivar, S.M. Janicki, and R.A. Greenberg. 2010. ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks. Cell. 141:970-981. http://dx.doi.org/10.1016/j.cell.2010.04.038
    • (2010) Cell , vol.141 , pp. 970-981
    • Shanbhag, N.M.1    Rafalska-Metcalf, I.U.2    Balane-Bolivar, C.3    Janicki, S.M.4    Greenberg, R.A.5
  • 51
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y., F. Lan, C. Matson, P. Mulligan, J.R. Whetstine, P.A. Cole, R.A. Casero, and Y. Shi. 2004. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell. 119:941-953. http://dx.doi.org/10.1016/j.cell.2004.12.012
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 52
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • Shi, Y.J., C. Matson, F. Lan, S. Iwase, T. Baba, and Y. Shi. 2005. Regulation of LSD1 histone demethylase activity by its associated factors. Mol. Cell. 19:857-864. http://dx.doi.org/10.1016/j.molcel.2005.08.027
    • (2005) Mol. Cell , vol.19 , pp. 857-864
    • Shi, Y.J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 53
    • 77956387556 scopus 로고    scopus 로고
    • The NuRD chromatin-remodeling complex regulates signaling and repair of DNA damage
    • Smeenk, G., W.W. Wiegant, H. Vrolijk, A.P. Solari, A. Pastink, and H. van Attikum. 2010. The NuRD chromatin-remodeling complex regulates signaling and repair of DNA damage. J. Cell Biol. 190:741-749. http://dx.doi.org/10.1083/jcb.201001048
    • (2010) J. Cell Biol , vol.190 , pp. 741-749
    • Smeenk, G.1    Wiegant, W.W.2    Vrolijk, H.3    Solari, A.P.4    Pastink, A.5    van Attikum, H.6
  • 54
    • 84872249432 scopus 로고    scopus 로고
    • Spp1, a member of the Set1 complex, promotes meiotic DSB formation in promoters by tethering histone H3K4 methylation sites to chromosome axes
    • Sommermeyer, V., C. Béneut, E. Chaplais, M.E. Serrentino, and V. Borde. 2013. Spp1, a member of the Set1 complex, promotes meiotic DSB formation in promoters by tethering histone H3K4 methylation sites to chromosome axes. Mol. Cell. 49:43-54.
    • (2013) Mol. Cell , vol.49 , pp. 43-54
    • Sommermeyer, V.1    Béneut, C.2    Chaplais, E.3    Serrentino, M.E.4    Borde, V.5
  • 55
    • 0037468192 scopus 로고    scopus 로고
    • MDC1 is a mediator of the mammalian DNA damage checkpoint
    • Stewart, G.S., B. Wang, C.R. Bignell, A.M. Taylor, and S.J. Elledge. 2003. MDC1 is a mediator of the mammalian DNA damage checkpoint. Nature. 421:961-966. http://dx.doi.org/10.1038/nature01446
    • (2003) Nature , vol.421 , pp. 961-966
    • Stewart, G.S.1    Wang, B.2    Bignell, C.R.3    Taylor, A.M.4    Elledge, S.J.5
  • 57
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D., and C.D. Allis. 2000. The language of covalent histone modifications. Nature. 403:41-45. http://dx.doi.org/10.1038/47412
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 58
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • Stucki, M., J.A. Clapperton, D. Mohammad, M.B. Yaffe, S.J. Smerdon, and S.P. Jackson. 2005. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell. 123:1213-1226. http://dx.doi.org/10.1016/j.cell.2005.09.038
    • (2005) Cell , vol.123 , pp. 1213-1226
    • Stucki, M.1    Clapperton, J.A.2    Mohammad, D.3    Yaffe, M.B.4    Smerdon, S.J.5    Jackson, S.P.6
  • 60
    • 65149084552 scopus 로고    scopus 로고
    • Crosstalk between histone modifications during the DNA damage response
    • van Attikum, H., and S.M. Gasser. 2009. Crosstalk between histone modifications during the DNA damage response. Trends Cell Biol. 19:207-217. http://dx.doi.org/10.1016/j.tcb.2009.03.001
    • (2009) Trends Cell Biol , vol.19 , pp. 207-217
    • van Attikum, H.1    Gasser, S.M.2
  • 63
    • 68749108259 scopus 로고    scopus 로고
    • LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer
    • Wang, Y., H. Zhang, Y. Chen, Y. Sun, F. Yang, W. Yu, J. Liang, L. Sun, X. Yang, L. Shi, et al. 2009. LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. Cell. 138:660-672. http://dx.doi.org/10.1016/j.cell.2009.05.050
    • (2009) Cell , vol.138 , pp. 660-672
    • Wang, Y.1    Zhang, H.2    Chen, Y.3    Sun, Y.4    Yang, F.5    Yu, W.6    Liang, J.7    Sun, L.8    Yang, X.9    Shi, L.10
  • 65
    • 33745221412 scopus 로고    scopus 로고
    • Assaying double-strand break repair pathway choice in mammalian cells using a targeted endonuclease or the RAG recombinase
    • Weinstock, D.M., K. Nakanishi, H.R. Helgadottir, and M. Jasin. 2006. Assaying double-strand break repair pathway choice in mammalian cells using a targeted endonuclease or the RAG recombinase. Methods Enzymol. 409:524-540. http://dx.doi.org/10.1016/S0076-6879(05)09031-2
    • (2006) Methods Enzymol , vol.409 , pp. 524-540
    • Weinstock, D.M.1    Nakanishi, K.2    Helgadottir, H.R.3    Jasin, M.4
  • 66
    • 37349096996 scopus 로고    scopus 로고
    • Distinct roles of chromatin-associated proteins MDC1 and 53BP1 in mammalian double-strand break repair
    • Xie, A., A. Hartlerode, M. Stucki, S. Odate, N. Puget, A. Kwok, G. Nagaraju, C. Yan, F.W. Alt, J. Chen, et al. 2007. Distinct roles of chromatin-associated proteins MDC1 and 53BP1 in mammalian double-strand break repair. Mol. Cell. 28:1045-1057. http://dx.doi.org/10.1016/j.molcel.2007.12.005
    • (2007) Mol. Cell , vol.28 , pp. 1045-1057
    • Xie, A.1    Hartlerode, A.2    Stucki, M.3    Odate, S.4    Puget, N.5    Kwok, A.6    Nagaraju, G.7    Yan, C.8    Alt, F.W.9    Chen, J.10
  • 67
    • 33746435258 scopus 로고    scopus 로고
    • Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase
    • Yang, M., C.B. Gocke, X. Luo, D. Borek, D.R. Tomchick, M. Machius, Z. Otwinowski, and H. Yu. 2006. Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol. Cell. 23:377-387. http://dx.doi.org/10.1016/j.molcel.2006.07.012
    • (2006) Mol. Cell , vol.23 , pp. 377-387
    • Yang, M.1    Gocke, C.B.2    Luo, X.3    Borek, D.4    Tomchick, D.R.5    Machius, M.6    Otwinowski, Z.7    Yu, H.8
  • 68
    • 0035852637 scopus 로고    scopus 로고
    • CoREST is an integral component of the CoREST-human histone deacetylase complex
    • You, A., J.K. Tong, C.M. Grozinger, and S.L. Schreiber. 2001. CoREST is an integral component of the CoREST-human histone deacetylase complex. Proc. Natl. Acad. Sci. USA. 98:1454-1458. http://dx.doi.org/10.1073/pnas.98.4.1454
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1454-1458
    • You, A.1    Tong, J.K.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 69
    • 77249142841 scopus 로고    scopus 로고
    • Alternative splicing of the histone demethylase LSD1/KDM1 contributes to the modulation of neurite morphogenesis in the mammalian nervous system
    • Zibetti, C., A. Adamo, C. Binda, F. Forneris, E. Toffolo, C. Verpilli, E. Ginellli, A. Mattevi, C. Sala, and E. Battaglioli. 2010. Alternative splicing of the histone demethylase LSD1/KDM1 contributes to the modulation of neurite morphogenesis in the mammalian nervous system. J. Neurosci. 30:2521-2532. http://dx.doi.org/10.1523/JNEUROSCI.5500-09.2010
    • (2010) J. Neurosci , vol.30 , pp. 2521-2532
    • Zibetti, C.1    Adamo, A.2    Binda, C.3    Forneris, F.4    Toffolo, E.5    Verpilli, C.6    Ginellli, E.7    Mattevi, A.8    Sala, C.9    Battaglioli, E.10


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