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Volumn 17, Issue 6, 2016, Pages 379-394

Regulation of DNA double-strand break repair by ubiquitin and ubiquitin-like modifiers

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 84969963406     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm.2016.58     Document Type: Review
Times cited : (292)

References (171)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. Instability and decay of the primary structure of DNA. Nature 362, 709-715 (1993).
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • Jackson, S. P. & Bartek, J. The DNA-damage response in human biology and disease. Nature 461, 1071-1078 (2009).
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 3
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • Hoeijmakers, J. H. Genome maintenance mechanisms for preventing cancer. Nature 411, 366-374 (2001).
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 4
    • 84873320525 scopus 로고    scopus 로고
    • Mechanisms of programmed DNA lesions and genomic instability in the immune system
    • Alt, F. W., Zhang, Y., Meng, F. L., Guo, C. & Schwer, B. Mechanisms of programmed DNA lesions and genomic instability in the immune system. Cell 152, 417-429 (2013).
    • (2013) Cell , vol.152 , pp. 417-429
    • Alt, F.W.1    Zhang, Y.2    Meng, F.L.3    Guo, C.4    Schwer, B.5
  • 5
    • 78649336706 scopus 로고    scopus 로고
    • The DNA damage response: Making it safe to play with knives
    • Ciccia, A. & Elledge, S. J. The DNA damage response: making it safe to play with knives. Mol. Cell 40, 179-204 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 179-204
    • Ciccia, A.1    Elledge, S.J.2
  • 6
    • 77953229115 scopus 로고    scopus 로고
    • The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway
    • Lieber, M. R. The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway. Annu. Rev. Biochem. 79, 181-211 (2010).
    • (2010) Annu. Rev. Biochem , vol.79 , pp. 181-211
    • Lieber, M.R.1
  • 7
    • 78149425175 scopus 로고    scopus 로고
    • Regulation of homologous recombination in eukaryotes
    • Heyer, W. D., Ehmsen, K. T. & Liu, J. Regulation of homologous recombination in eukaryotes. Annu. Rev. Genet. 44, 113-139 (2010).
    • (2010) Annu. Rev. Genet , vol.44 , pp. 113-139
    • Heyer, W.D.1    Ehmsen, K.T.2    Liu, J.3
  • 8
    • 84865364870 scopus 로고    scopus 로고
    • Playing the end game: DNA double-strand break repair pathway choice
    • Chapman, J. R., Taylor, M. R. & Boulton, S. J. Playing the end game: DNA double-strand break repair pathway choice. Mol. Cell 47, 497-510 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 497-510
    • Chapman, J.R.1    Taylor, M.R.2    Boulton, S.J.3
  • 9
    • 84876886904 scopus 로고    scopus 로고
    • Regulation of DNA damage responses by ubiquitin and SUMO
    • Jackson, S. P. & Durocher, D. Regulation of DNA damage responses by ubiquitin and SUMO. Mol. Cell 49, 795-807 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 795-807
    • Jackson, S.P.1    Durocher, D.2
  • 10
    • 80052697814 scopus 로고    scopus 로고
    • The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks
    • Bekker-Jensen, S. & Mailand, N. The ubiquitin- and SUMO-dependent signaling response to DNA double-strand breaks. FEBS Lett. 585, 2914-2919 (2011).
    • (2011) FEBS Lett , vol.585 , pp. 2914-2919
    • Bekker-Jensen, S.1    Mailand, N.2
  • 11
    • 82455179484 scopus 로고    scopus 로고
    • Systematic and quantitative assessment of the ubiquitin-modified proteome
    • Kim, W. et al. Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol. Cell 44, 325-340 (2011).
    • (2011) Mol. Cell , vol.44 , pp. 325-340
    • Kim, W.1
  • 12
    • 80054033461 scopus 로고    scopus 로고
    • A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles
    • M111.013284
    • Wagner, S. A. et al. A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol. Cell. Proteomics 10, M111.013284 (2011).
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wagner, S.A.1
  • 14
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander, D., Clague, M. J. & Urbe, S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 10, 550-563 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 15
    • 84922010371 scopus 로고    scopus 로고
    • Systematic characterization of deubiquitylating enzymes for roles in maintaining genome integrity
    • Nishi, R. et al. Systematic characterization of deubiquitylating enzymes for roles in maintaining genome integrity. Nat. Cell Biol. 16, 1016-1026 (2014).
    • (2014) Nat. Cell Biol , vol.16 , pp. 1016-1026
    • Nishi, R.1
  • 16
    • 84945937533 scopus 로고    scopus 로고
    • Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting DNA repair
    • Schmidt, C. K. et al. Systematic E2 screening reveals a UBE2D-RNF138-CtIP axis promoting DNA repair. Nat. Cell Biol. 17, 1458-1470 (2015).
    • (2015) Nat. Cell Biol , vol.17 , pp. 1458-1470
    • Schmidt, C.K.1
  • 17
    • 84940897506 scopus 로고    scopus 로고
    • Quantitative proteomic atlas of ubiquitination and acetylation in the DNA damage response
    • Elia, A. E. et al. Quantitative proteomic atlas of ubiquitination and acetylation in the DNA damage response. Mol. Cell 59, 867-881 (2015).
    • (2015) Mol. Cell , vol.59 , pp. 867-881
    • Elia, A.E.1
  • 19
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J. R. & Lima, C. D. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat. Rev. Mol. Cell Biol. 11, 861-871 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 20
    • 84925775745 scopus 로고    scopus 로고
    • Uncovering global SUMOylation signaling networks in a site-specific manner
    • Hendriks, I. A. et al. Uncovering global SUMOylation signaling networks in a site-specific manner. Nat. Struct. Mol. Biol. 21, 927-936 (2014).
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 927-936
    • Hendriks, I.A.1
  • 21
    • 36249031962 scopus 로고    scopus 로고
    • RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly
    • Huen, M. S. et al. RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. Cell 131, 901-914 (2007).
    • (2007) Cell , vol.131 , pp. 901-914
    • Huen, M.S.1
  • 22
    • 1942517849 scopus 로고    scopus 로고
    • BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair
    • Morris, J. R. & Solomon, E. BRCA1: BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair. Hum. Mol. Genet. 13, 807-817 (2004).
    • (2004) Hum. Mol. Genet , vol.13 , pp. 807-817
    • Morris, J.R.1    Solomon, E.2
  • 23
    • 84920936909 scopus 로고    scopus 로고
    • RNF168 promotes noncanonical K27 ubiquitination to signal DNA damage
    • Gatti, M. et al. RNF168 promotes noncanonical K27 ubiquitination to signal DNA damage. Cell Rep. 10, 226-238 (2015).
    • (2015) Cell Rep , vol.10 , pp. 226-238
    • Gatti, M.1
  • 24
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9
    • Tatham, M. H. et al. Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J. Biol. Chem. 276, 35368-35374 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 35368-35374
    • Tatham, M.H.1
  • 25
    • 70349441058 scopus 로고    scopus 로고
    • Ubiquitin-binding domains - From structures to functions
    • Dikic, I., Wakatsuki, S. & Walters, K. J. Ubiquitin-binding domains - from structures to functions. Nat. Rev. Mol. Cell Biol. 10, 659-671 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 659-671
    • Dikic, I.1    Wakatsuki, S.2    Walters, K.J.3
  • 26
    • 62549161305 scopus 로고    scopus 로고
    • Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of Rap80
    • Sims, J. J. & Cohen, R. E. Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of Rap80. Mol. Cell 33, 775-783 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 775-783
    • Sims, J.J.1    Cohen, R.E.2
  • 27
    • 69149088033 scopus 로고    scopus 로고
    • Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80
    • Sato, Y. et al. Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80. EMBO J. 28, 2461-2468 (2009).
    • (2009) EMBO J , vol.28 , pp. 2461-2468
    • Sato, Y.1
  • 28
    • 84864919890 scopus 로고    scopus 로고
    • Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks
    • Panier, S. et al. Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks. Mol. Cell 47, 383-395 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 383-395
    • Panier, S.1
  • 29
    • 84879888213 scopus 로고    scopus 로고
    • 53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
    • Fradet-Turcotte, A. et al. 53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark. Nature 499, 50-54 (2013). Reveals that 53BP1 contains a UDR domain that directly recognizes RNF168-ubiquitylated H2A and mediates its recruitment to DSBs.
    • (2013) Nature , vol.499 , pp. 50-54
    • Fradet-Turcotte, A.1
  • 30
  • 31
    • 78649450619 scopus 로고    scopus 로고
    • Assembly and function of DNA double-strand break repair foci in mammalian cells
    • Bekker-Jensen, S. & Mailand, N. Assembly and function of DNA double-strand break repair foci in mammalian cells. DNA Repair 9, 1219-1228 (2010).
    • (2010) DNA Repair , vol.9 , pp. 1219-1228
    • Bekker-Jensen, S.1    Mailand, N.2
  • 32
    • 80053555789 scopus 로고    scopus 로고
    • More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance
    • Lukas, J., Lukas, C. & Bartek, J. More than just a focus: the chromatin response to DNA damage and its role in genome integrity maintenance. Nat. Cell Biol. 13, 1161-1169 (2011).
    • (2011) Nat. Cell Biol , vol.13 , pp. 1161-1169
    • Lukas, J.1    Lukas, C.2    Bartek, J.3
  • 33
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand, N. et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 131, 887-900 (2007).
    • (2007) Cell , vol.131 , pp. 887-900
    • Mailand, N.1
  • 34
    • 36749084931 scopus 로고    scopus 로고
    • Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase
    • Kolas, N. K. et al. Orchestration of the DNA-damage response by the RNF8 ubiquitin ligase. Science 318, 1637-1640 (2007).
    • (2007) Science , vol.318 , pp. 1637-1640
    • Kolas, N.K.1
  • 35
    • 59049091728 scopus 로고    scopus 로고
    • RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins
    • Doil, C. et al. RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins. Cell 136, 435-446 (2009).
    • (2009) Cell , vol.136 , pp. 435-446
    • Doil, C.1
  • 36
    • 59049103900 scopus 로고    scopus 로고
    • The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage
    • Stewart, G. S. et al. The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage. Cell 136, 420-434 (2009).
    • (2009) Cell , vol.136 , pp. 420-434
    • Stewart, G.S.1
  • 37
    • 36749025467 scopus 로고    scopus 로고
    • Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage
    • Wang, B. & Elledge, S. J. Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage. Proc. Natl Acad. Sci. USA 104, 20759-20763 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20759-20763
    • Wang, B.1    Elledge, S.J.2
  • 38
    • 77953720192 scopus 로고    scopus 로고
    • ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks
    • Shanbhag, N. M., Rafalska-Metcalf, I. U., Balane-Bolivar, C., Janicki, S. M. & Greenberg, R. A. ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks. Cell 141, 970-981(2010).
    • (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
  • 39
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • Stucki, M. et al. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell 123, 1213-1226 (2005).
    • (2005) Cell , vol.123 , pp. 1213-1226
    • Stucki, M.1
  • 40
    • 84866388311 scopus 로고    scopus 로고
    • RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling
    • Mattiroli, F. et al. RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling. Cell 150, 1182-1195 (2012).
    • (2012) Cell , vol.150 , pp. 1182-1195
    • Mattiroli, F.1
  • 41
    • 84863793933 scopus 로고    scopus 로고
    • A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase
    • Gatti, M. et al. A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase. Cell Cycle 11, 2538-2544 (2012).
    • (2012) Cell Cycle , vol.11 , pp. 2538-2544
    • Gatti, M.1
  • 42
    • 84898725334 scopus 로고    scopus 로고
    • The nucleosome acidic patch plays a critical role in RNF168-dependent ubiquitination of histone H2A
    • Mattiroli, F., Uckelmann, M., Sahtoe, D. D., van Dijk, W. J. & Sixma, T. K. The nucleosome acidic patch plays a critical role in RNF168-dependent ubiquitination of histone H2A. Nat. Commun. 5, 3291 (2014).
    • (2014) Nat. Commun , vol.5 , pp. 3291
    • Mattiroli, F.1    Uckelmann, M.2    Sahtoe, D.D.3    Van Dijk, W.J.4    Sixma, T.K.5
  • 43
    • 84897449829 scopus 로고    scopus 로고
    • Nucleosome acidic patch promotes RNF168- and RING1B/BMI1-dependent H2AX and H2A ubiquitination and DNA damage signaling
    • Leung, J. W. et al. Nucleosome acidic patch promotes RNF168- and RING1B/BMI1-dependent H2AX and H2A ubiquitination and DNA damage signaling. PLoS Genet. 10, e1004178 (2014).
    • (2014) PLoS Genet , vol.10
    • Leung, J.W.1
  • 44
    • 84946079065 scopus 로고    scopus 로고
    • Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage
    • Thorslund, T. et al. Histone H1 couples initiation and amplification of ubiquitin signalling after DNA damage. Nature 527, 389-393 (2015). Discovery that RNF8 promotes K63-linked ubiquitylation of H1-type histones to promote recruitment of RNF168.
    • (2015) Nature , vol.527 , pp. 389-393
    • Thorslund, T.1
  • 45
    • 84862986431 scopus 로고    scopus 로고
    • HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes
    • Bekker-Jensen, S. et al. HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes. Nat. Cell Biol. 12, 80-86 (2010).
    • (2010) Nat. Cell Biol , vol.12 , pp. 80-86
    • Bekker-Jensen, S.1
  • 47
    • 84929102368 scopus 로고    scopus 로고
    • Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links
    • Raschle, M. et al. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. Science 348, 1253671 (2015).
    • (2015) Science , vol.348
    • Raschle, M.1
  • 48
    • 67349168142 scopus 로고    scopus 로고
    • RAD18 transmits DNA damage signalling to elicit homologous recombination repair
    • Huang, J. et al. RAD18 transmits DNA damage signalling to elicit homologous recombination repair. Nat. Cell Biol. 11, 592-603 (2009).
    • (2009) Nat. Cell Biol , vol.11 , pp. 592-603
    • Huang, J.1
  • 49
    • 84861948252 scopus 로고    scopus 로고
    • Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks
    • Poulsen, M., Lukas, C., Lukas, J., Bekker-Jensen, S. & Mailand, N. Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks. J. Cell Biol. 197, 189-199 (2012).
    • (2012) J. Cell Biol , vol.197 , pp. 189-199
    • Poulsen, M.1    Lukas, C.2    Lukas, J.3    Bekker-Jensen, S.4    Mailand, N.5
  • 50
    • 84864977706 scopus 로고    scopus 로고
    • Ring finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damage
    • Chen, J., Feng, W., Jiang, J., Deng, Y. & Huen, M. S. Ring finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damage. J. Biol. Chem. 287, 27715-27722 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 27715-27722
    • Chen, J.1    Feng, W.2    Jiang, J.3    Deng, Y.4    Huen, M.S.5
  • 51
    • 33646808638 scopus 로고    scopus 로고
    • A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites
    • Polanowska, J., Martin, J. S., Garcia-Muse, T., Petalcorin, M. I. & Boulton, S. J. A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA damage sites. EMBO J. 25, 2178-2188 (2006).
    • (2006) EMBO J , vol.25 , pp. 2178-2188
    • Polanowska, J.1    Martin, J.S.2    Garcia-Muse, T.3    Petalcorin, M.I.4    Boulton, S.J.5
  • 52
    • 79951974992 scopus 로고    scopus 로고
    • Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks
    • Moyal, L. et al. Requirement of ATM-dependent monoubiquitylation of histone H2B for timely repair of DNA double-strand breaks. Mol. Cell 41, 529-542 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 529-542
    • Moyal, L.1
  • 53
    • 79951971464 scopus 로고    scopus 로고
    • Regulation of homologous recombination by RNF20-dependent H2B ubiquitination
    • Nakamura, K. et al. Regulation of homologous recombination by RNF20-dependent H2B ubiquitination. Mol. Cell 41, 515-528 (2011).
    • (2011) Mol. Cell , vol.41 , pp. 515-528
    • Nakamura, K.1
  • 54
    • 77957748289 scopus 로고    scopus 로고
    • BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair
    • Ismail, I. H., Andrin, C., McDonald, D. & Hendzel, M. J. BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair. J. Cell Biol. 191, 45-60 (2010).
    • (2010) J. Cell Biol , vol.191 , pp. 45-60
    • Ismail, I.H.1    Andrin, C.2    McDonald, D.3    Hendzel, M.J.4
  • 55
    • 79956086415 scopus 로고    scopus 로고
    • BMI1 is recruited to DNA breaks and contributes to DNA damage-induced H2A ubiquitination and repair
    • Ginjala, V. et al. BMI1 is recruited to DNA breaks and contributes to DNA damage-induced H2A ubiquitination and repair. Mol. Cell. Biol. 31, 1972-1982 (2011).
    • (2011) Mol. Cell. Biol , vol.31 , pp. 1972-1982
    • Ginjala, V.1
  • 56
    • 80051494784 scopus 로고    scopus 로고
    • Monoubiquitination of H2AX protein regulates DNA damage response signaling
    • Pan, M. R., Peng, G., Hung, W. C. & Lin, S. Y. Monoubiquitination of H2AX protein regulates DNA damage response signaling. J. Biol. Chem. 286, 28599-28607 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 28599-28607
    • Pan, M.R.1    Peng, G.2    Hung, W.C.3    Lin, S.Y.4
  • 57
    • 84873631924 scopus 로고    scopus 로고
    • CHFR is important for the first wave of ubiquitination at DNA damage sites
    • Liu, C., Wu, J., Paudyal, S. C., You, Z. & Yu, X. CHFR is important for the first wave of ubiquitination at DNA damage sites. Nucleic Acids Res. 41, 1698-1710 (2013).
    • (2013) Nucleic Acids Res , vol.41 , pp. 1698-1710
    • Liu, C.1    Wu, J.2    Paudyal, S.C.3    You, Z.4    Yu, X.5
  • 58
    • 33646117239 scopus 로고    scopus 로고
    • Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks
    • Bekker-Jensen, S. et al. Spatial organization of the mammalian genome surveillance machinery in response to DNA strand breaks. J. Cell Biol. 173, 195-206 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 195-206
    • Bekker-Jensen, S.1
  • 59
    • 84892895021 scopus 로고    scopus 로고
    • PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry
    • Marechal, A. et al. PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry. Mol. Cell 53, 235-246 (2014).
    • (2014) Mol. Cell , vol.53 , pp. 235-246
    • Marechal, A.1
  • 60
    • 84944893122 scopus 로고    scopus 로고
    • RFWD3-dependent ubiquitination of RPA regulates repair at stalled replication forks
    • Elia, A. E. et al. RFWD3-dependent ubiquitination of RPA regulates repair at stalled replication forks. Mol. Cell 60, 280-293 (2015).
    • (2015) Mol. Cell , vol.60 , pp. 280-293
    • Elia, A.E.1
  • 61
    • 84945973395 scopus 로고    scopus 로고
    • The RNF138 E3 ligase displaces Ku to promote DNA end resection and regulate DNA repair pathway choice
    • Ismail, I. H. et al. The RNF138 E3 ligase displaces Ku to promote DNA end resection and regulate DNA repair pathway choice. Nat. Cell Biol. 17, 1446-1457 (2015).
    • (2015) Nat. Cell Biol , vol.17 , pp. 1446-1457
    • Ismail, I.H.1
  • 62
    • 84886429265 scopus 로고    scopus 로고
    • Push back to respond better: Regulatory inhibition of the DNA double-strand break response
    • Panier, S. & Durocher, D. Push back to respond better: regulatory inhibition of the DNA double-strand break response. Nat. Rev. Mol. Cell Biol. 14, 661-672 (2013).
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 661-672
    • Panier, S.1    Durocher, D.2
  • 63
    • 84865232294 scopus 로고    scopus 로고
    • TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes
    • Gudjonsson, T. et al. TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes. Cell 150, 697-709 (2012).
    • (2012) Cell , vol.150 , pp. 697-709
    • Gudjonsson, T.1
  • 64
    • 36049036216 scopus 로고    scopus 로고
    • Human USP3 is a chromatin modifier required for S phase progression and genome stability
    • Nicassio, F. et al. Human USP3 is a chromatin modifier required for S phase progression and genome stability. Curr. Biol. 17, 1972-1977 (2007).
    • (2007) Curr. Biol , vol.17 , pp. 1972-1977
    • Nicassio, F.1
  • 65
    • 84878758649 scopus 로고    scopus 로고
    • The deubiquitylating enzyme USP44 counteracts the DNA double-strand break response mediated by the RNF8 and RNF168 ubiquitin ligases
    • Mosbech, A., Lukas, C., Bekker-Jensen, S. & Mailand, N. The deubiquitylating enzyme USP44 counteracts the DNA double-strand break response mediated by the RNF8 and RNF168 ubiquitin ligases. J. Biol. Chem. 288, 16579-16587 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 16579-16587
    • Mosbech, A.1    Lukas, C.2    Bekker-Jensen, S.3    Mailand, N.4
  • 66
    • 84892562030 scopus 로고    scopus 로고
    • USP3 counteracts RNF168 via deubiquitinating H2A and γh2AX at lysine 13 and 15
    • Sharma, N. et al. USP3 counteracts RNF168 via deubiquitinating H2A and γH2AX at lysine 13 and 15. Cell Cycle 13, 106-114 (2014).
    • (2014) Cell Cycle , vol.13 , pp. 106-114
    • Sharma, N.1
  • 67
    • 84906552235 scopus 로고    scopus 로고
    • Tight regulation of ubiquitin-mediated DNA damage response by USP3 preserves the functional integrity of hematopoietic stem cells
    • Lancini, C. et al. Tight regulation of ubiquitin-mediated DNA damage response by USP3 preserves the functional integrity of hematopoietic stem cells. J. Exp. Med. 211, 1759-1777 (2014).
    • (2014) J. Exp. Med , vol.211 , pp. 1759-1777
    • Lancini, C.1
  • 68
    • 77955867565 scopus 로고    scopus 로고
    • Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1
    • Nakada, S. et al. Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1. Nature 466, 941-946 (2010).
    • (2010) Nature , vol.466 , pp. 941-946
    • Nakada, S.1
  • 69
    • 84856801739 scopus 로고    scopus 로고
    • OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function
    • Juang, Y. C. et al. OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function. Mol. Cell 45, 384-397 (2012).
    • (2012) Mol. Cell , vol.45 , pp. 384-397
    • Juang, Y.C.1
  • 70
    • 62549140202 scopus 로고    scopus 로고
    • The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks
    • Shao, G. et al. The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks. Proc. Natl Acad. Sci. USA 106, 3166-3171 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 3166-3171
    • Shao, G.1
  • 71
    • 84894067659 scopus 로고    scopus 로고
    • Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice
    • Kato, K. et al. Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice. Mol. Cell 53, 617-630 (2014).
    • (2014) Mol. Cell , vol.53 , pp. 617-630
    • Kato, K.1
  • 72
    • 84867101138 scopus 로고    scopus 로고
    • The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response
    • Butler, L. R. et al. The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response. EMBO J. 31, 3918-3934 (2012).
    • (2012) EMBO J , vol.31 , pp. 3918-3934
    • Butler, L.R.1
  • 73
    • 80455145246 scopus 로고    scopus 로고
    • The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks
    • Meerang, M. et al. The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks. Nat. Cell Biol. 13, 1376-1382 (2011).
    • (2011) Nat. Cell Biol , vol.13 , pp. 1376-1382
    • Meerang, M.1
  • 74
    • 84861765707 scopus 로고    scopus 로고
    • RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair
    • Galanty, Y., Belotserkovskaya, R., Coates, J. & Jackson, S. P. RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair. Genes Dev. 26, 1179-1195 (2012).
    • (2012) Genes Dev , vol.26 , pp. 1179-1195
    • Galanty, Y.1    Belotserkovskaya, R.2    Coates, J.3    Jackson, S.P.4
  • 75
    • 82955233157 scopus 로고    scopus 로고
    • The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
    • Acs, K. et al. The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks. Nat. Struct. Mol. Biol. 18, 1345-1350 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 1345-1350
    • Acs, K.1
  • 76
    • 77954997032 scopus 로고    scopus 로고
    • DNA damage signaling in response to double-strand breaks during mitosis
    • Giunta, S., Belotserkovskaya, R. & Jackson, S. P. DNA damage signaling in response to double-strand breaks during mitosis. J. Cell Biol. 190, 197-207 (2010).
    • (2010) J. Cell Biol , vol.190 , pp. 197-207
    • Giunta, S.1    Belotserkovskaya, R.2    Jackson, S.P.3
  • 77
    • 84898052474 scopus 로고    scopus 로고
    • Mitosis inhibits DNA double-strand break repair to guard against telomere fusions
    • Orthwein, A. et al. Mitosis inhibits DNA double-strand break repair to guard against telomere fusions. Science 344, 189-193 (2014). Shows that the RNF8-RNF168-mediated DSB response is inactivated during mitosis to suppress telomere fusions and genomic instability.
    • (2014) Science , vol.344 , pp. 189-193
    • Orthwein, A.1
  • 78
    • 80052491304 scopus 로고    scopus 로고
    • DNA-damage response and repair activities at uncapped telomeres depend on RNF8
    • Peuscher, M. H. & Jacobs, J. J. DNA-damage response and repair activities at uncapped telomeres depend on RNF8. Nat. Cell Biol. 13, 1139-1145 (2011).
    • (2011) Nat. Cell Biol , vol.13 , pp. 1139-1145
    • Peuscher, M.H.1    Jacobs, J.J.2
  • 79
    • 84874351566 scopus 로고    scopus 로고
    • A two-step mechanism for TRF2-mediated chromosome-end protection
    • Okamoto, K. et al. A two-step mechanism for TRF2-mediated chromosome-end protection. Nature 494, 502-505 (2013).
    • (2013) Nature , vol.494 , pp. 502-505
    • Okamoto, K.1
  • 80
    • 84930948486 scopus 로고    scopus 로고
    • Phosphorylation of EXO1 by CDKs 1 and 2 regulates DNA end resection and repair pathway choice
    • Tomimatsu, N. et al. Phosphorylation of EXO1 by CDKs 1 and 2 regulates DNA end resection and repair pathway choice. Nat. Commun. 5, 3561 (2014).
    • (2014) Nat. Commun , vol.5 , pp. 3561
    • Tomimatsu, N.1
  • 81
    • 84919359385 scopus 로고    scopus 로고
    • APC/CCdh1 controls CtIP stability during the cell cycle and in response to DNA damage
    • Lafranchi, L. et al. APC/CCdh1 controls CtIP stability during the cell cycle and in response to DNA damage. EMBO J. 33, 2860-2879 (2014).
    • (2014) EMBO J , vol.33 , pp. 2860-2879
    • Lafranchi, L.1
  • 82
    • 84862777619 scopus 로고    scopus 로고
    • The E3 ligase RNF8 regulates KU80 removal and NHEJ repair
    • Feng, L. & Chen, J. The E3 ligase RNF8 regulates KU80 removal and NHEJ repair. Nat. Struct. Mol. Biol. 19, 201-206 (2012).
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 201-206
    • Feng, L.1    Chen, J.2
  • 83
    • 84874609470 scopus 로고    scopus 로고
    • An SCF complex containing Fbxl12 mediates DNA damage-induced Ku80 ubiquitylation
    • Postow, L. & Funabiki, H. An SCF complex containing Fbxl12 mediates DNA damage-induced Ku80 ubiquitylation. Cell Cycle 12, 587-595 (2013).
    • (2013) Cell Cycle , vol.12 , pp. 587-595
    • Postow, L.1    Funabiki, H.2
  • 84
    • 84947815576 scopus 로고    scopus 로고
    • USP4 auto-deubiquitylation promotes homologous recombination
    • Wijnhoven, P. et al. USP4 auto-deubiquitylation promotes homologous recombination. Mol. Cell 60, 362-373 (2015).
    • (2015) Mol. Cell , vol.60 , pp. 362-373
    • Wijnhoven, P.1
  • 85
    • 84943363184 scopus 로고    scopus 로고
    • The deubiquitylating enzyme USP4 cooperates with CtIP in DNA double-strand break end resection
    • Liu, H. et al. The deubiquitylating enzyme USP4 cooperates with CtIP in DNA double-strand break end resection. Cell Rep. 13, 93-107 (2015).
    • (2015) Cell Rep , vol.13 , pp. 93-107
    • Liu, H.1
  • 86
    • 34249949779 scopus 로고    scopus 로고
    • RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites
    • Sobhian, B. et al. RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sites. Science 316, 1198-1202 (2007).
    • (2007) Science , vol.316 , pp. 1198-1202
    • Sobhian, B.1
  • 87
    • 34249950879 scopus 로고    scopus 로고
    • Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response
    • Kim, H., Chen, J. & Yu, X. Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response. Science 316, 1202-1205 (2007).
    • (2007) Science , vol.316 , pp. 1202-1205
    • Kim, H.1    Chen, J.2    Yu, X.3
  • 88
    • 34249946686 scopus 로고    scopus 로고
    • Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response
    • Wang, B. et al. Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. Science 316, 1194-1198 (2007).
    • (2007) Science , vol.316 , pp. 1194-1198
    • Wang, B.1
  • 89
    • 59249095962 scopus 로고    scopus 로고
    • Histone ubiquitination associates with BRCA1-dependent DNA damage response
    • Wu, J. et al. Histone ubiquitination associates with BRCA1-dependent DNA damage response. Mol. Cell. Biol. 29, 849-860 (2009).
    • (2009) Mol. Cell. Biol , vol.29 , pp. 849-860
    • Wu, J.1
  • 90
    • 84891014338 scopus 로고    scopus 로고
    • Double-strand break repair: 53BP1 comes into focus
    • Panier, S. & Boulton, S. J. Double-strand break repair: 53BP1 comes into focus. Nat. Rev. Mol. Cell Biol. 15, 7-18 (2014).
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 7-18
    • Panier, S.1    Boulton, S.J.2
  • 91
    • 37549014575 scopus 로고    scopus 로고
    • Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle
    • Pesavento, J. J., Yang, H., Kelleher, N. L. & Mizzen, C. A. Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle. Mol. Cell. Biol. 28, 468-486 (2008).
    • (2008) Mol. Cell. Biol , vol.28 , pp. 468-486
    • Pesavento, J.J.1    Yang, H.2    Kelleher, N.L.3    Mizzen, C.A.4
  • 92
    • 84859895529 scopus 로고    scopus 로고
    • RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites
    • Mallette, F. A. et al. RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J. 31, 1865-1878 (2012).
    • (2012) EMBO J , vol.31 , pp. 1865-1878
    • Mallette, F.A.1
  • 93
    • 68949221567 scopus 로고    scopus 로고
    • A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency
    • Cao, L. et al. A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency. Mol. Cell 35, 534-541 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 534-541
    • Cao, L.1
  • 94
    • 77950958141 scopus 로고    scopus 로고
    • 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks
    • Bunting, S. F. et al. 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks. Cell 141, 243-254 (2010).
    • (2010) Cell , vol.141 , pp. 243-254
    • Bunting, S.F.1
  • 95
    • 77953291328 scopus 로고    scopus 로고
    • 53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers
    • Bouwman, P. et al. 53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers. Nat. Struct. Mol. Biol. 17, 688-695 (2010). References 94 and 95 demonstrate that 53BP1 inhibits DSB end resection and homologous recombination.
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 688-695
    • Bouwman, P.1
  • 96
    • 84876877091 scopus 로고    scopus 로고
    • A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and BRCA1-CtIP controls DNA repair pathway choice
    • Escribano-Diaz, C. et al. A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and BRCA1-CtIP controls DNA repair pathway choice. Mol. Cell 49, 872-883 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 872-883
    • Escribano-Diaz, C.1
  • 97
    • 84876855215 scopus 로고    scopus 로고
    • RIF1 is essential for 53BP1-dependent nonhomologous end joining and suppression of DNA double-strand break resection
    • Chapman, J. R. et al. RIF1 is essential for 53BP1-dependent nonhomologous end joining and suppression of DNA double-strand break resection. Mol. Cell 49, 858-871 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 858-871
    • Chapman, J.R.1
  • 98
    • 84873526612 scopus 로고    scopus 로고
    • Rif1 prevents resection of DNA breaks and promotes immunoglobulin class switching
    • Di Virgilio, M. et al. Rif1 prevents resection of DNA breaks and promotes immunoglobulin class switching. Science 339, 711-715 (2013).
    • (2013) Science , vol.339 , pp. 711-715
    • Di Virgilio, M.1
  • 100
    • 84930646986 scopus 로고    scopus 로고
    • MAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5' end resection
    • Boersma, V. et al. MAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5' end resection. Nature 521, 537-540 (2015).
    • (2015) Nature , vol.521 , pp. 537-540
    • Boersma, V.1
  • 101
    • 84930678981 scopus 로고    scopus 로고
    • REV7 counteracts DNA double-strand break resection and affects PARP inhibition
    • Xu, G. et al. REV7 counteracts DNA double-strand break resection and affects PARP inhibition. Nature 521, 541-544 (2015).
    • (2015) Nature , vol.521 , pp. 541-544
    • Xu, G.1
  • 102
    • 84890324730 scopus 로고    scopus 로고
    • Co-operation of BRCA1 and POH1 relieves the barriers posed by 53BP1 and RAP80 to resection
    • Kakarougkas, A. et al. Co-operation of BRCA1 and POH1 relieves the barriers posed by 53BP1 and RAP80 to resection. Nucleic Acids Res. 41, 10298-10311 (2013).
    • (2013) Nucleic Acids Res , vol.41 , pp. 10298-10311
    • Kakarougkas, A.1
  • 103
    • 84865386136 scopus 로고    scopus 로고
    • BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair
    • Chapman, J. R., Sossick, A. J., Boulton, S. J. & Jackson, S. P. BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair. J. Cell Sci. 125, 3529-3534 (2012).
    • (2012) J. Cell Sci , vol.125 , pp. 3529-3534
    • Chapman, J.R.1    Sossick, A.J.2    Boulton, S.J.3    Jackson, S.P.4
  • 104
    • 34548771748 scopus 로고    scopus 로고
    • Phospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damage
    • Munoz, I. M., Jowsey, P. A., Toth, R. & Rouse, J. Phospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damage. Nucleic Acids Res. 35, 5312-5322 (2007).
    • (2007) Nucleic Acids Res , vol.35 , pp. 5312-5322
    • Munoz, I.M.1    Jowsey, P.A.2    Toth, R.3    Rouse, J.4
  • 105
    • 84878893538 scopus 로고    scopus 로고
    • 53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions
    • Callen, E. et al. 53BP1 mediates productive and mutagenic DNA repair through distinct phosphoprotein interactions. Cell 153, 1266-1280 (2013).
    • (2013) Cell , vol.153 , pp. 1266-1280
    • Callen, E.1
  • 106
    • 84918555933 scopus 로고    scopus 로고
    • PTIP associates with Artemis to dictate DNA repair pathway choice
    • Wang, J. et al. PTIP associates with Artemis to dictate DNA repair pathway choice. Genes Dev. 28, 2693-2698 (2014).
    • (2014) Genes Dev , vol.28 , pp. 2693-2698
    • Wang, J.1
  • 107
    • 84878551708 scopus 로고    scopus 로고
    • The interaction between CtIP and BRCA1 is not essential for resection-mediated DNA repair or tumor suppression
    • Reczek, C. R., Szabolcs, M., Stark, J. M., Ludwig, T. & Baer, R. The interaction between CtIP and BRCA1 is not essential for resection-mediated DNA repair or tumor suppression. J. Cell Biol. 201, 693-707 (2013).
    • (2013) J. Cell Biol , vol.201 , pp. 693-707
    • Reczek, C.R.1    Szabolcs, M.2    Stark, J.M.3    Ludwig, T.4    Baer, R.5
  • 108
    • 84901766946 scopus 로고    scopus 로고
    • CtIP-mediated resection is essential for viability and can operate independently of BRCA1
    • Polato, F. et al. CtIP-mediated resection is essential for viability and can operate independently of BRCA1. J. Exp. Med. 211, 1027-1036 (2014).
    • (2014) J. Exp. Med , vol.211 , pp. 1027-1036
    • Polato, F.1
  • 109
    • 84919839708 scopus 로고    scopus 로고
    • BRCA1 accelerates CtIP-mediated DNA-end resection
    • Cruz-Garcia, A., Lopez-Saavedra, A. & Huertas, P. BRCA1 accelerates CtIP-mediated DNA-end resection. Cell Rep. 9, 451-459 (2014).
    • (2014) Cell Rep , vol.9 , pp. 451-459
    • Cruz-Garcia, A.1    Lopez-Saavedra, A.2    Huertas, P.3
  • 110
    • 79953869356 scopus 로고    scopus 로고
    • The BRCA1-RAP80 complex regulates DNA repair mechanism utilization by restricting end resection
    • Coleman, K. A. & Greenberg, R. A. The BRCA1-RAP80 complex regulates DNA repair mechanism utilization by restricting end resection. J. Biol. Chem. 286, 13669-13680 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 13669-13680
    • Coleman, K.A.1    Greenberg, R.A.2
  • 111
    • 79954528832 scopus 로고    scopus 로고
    • RAP80-directed tuning of BRCA1 homologous recombination function at ionizing radiation-induced nuclear foci
    • Hu, Y. et al. RAP80-directed tuning of BRCA1 homologous recombination function at ionizing radiation-induced nuclear foci. Genes Dev. 25, 685-700 (2011).
    • (2011) Genes Dev , vol.25 , pp. 685-700
    • Hu, Y.1
  • 112
    • 80055092789 scopus 로고    scopus 로고
    • BRCA1 tumor suppression depends on BRCT phosphoprotein binding, but not its E3 ligase activity
    • Shakya, R. et al. BRCA1 tumor suppression depends on BRCT phosphoprotein binding, but not its E3 ligase activity. Science 334, 525-528 (2011).
    • (2011) Science , vol.334 , pp. 525-528
    • Shakya, R.1
  • 113
    • 83455229693 scopus 로고    scopus 로고
    • BRCA1 RING function is essential for tumor suppression but dispensable for therapy resistance
    • Drost, R. et al. BRCA1 RING function is essential for tumor suppression but dispensable for therapy resistance. Cancer Cell 20, 797-809 (2011).
    • (2011) Cancer Cell , vol.20 , pp. 797-809
    • Drost, R.1
  • 114
    • 33745614048 scopus 로고    scopus 로고
    • BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP
    • Yu, X., Fu, S., Lai, M., Baer, R. & Chen, J. BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP. Genes Dev. 20, 1721-1726 (2006).
    • (2006) Genes Dev , vol.20 , pp. 1721-1726
    • Yu, X.1    Fu, S.2    Lai, M.3    Baer, R.4    Chen, J.5
  • 115
    • 84908356633 scopus 로고    scopus 로고
    • BRCA1 is a histone-H2A-specific ubiquitin ligase
    • Kalb, R., Mallery, D. L., Larkin, C., Huang, J. T. & Hiom, K. BRCA1 is a histone-H2A-specific ubiquitin ligase. Cell Rep. 8, 999-1005 (2014).
    • (2014) Cell Rep , vol.8 , pp. 999-1005
    • Kalb, R.1    Mallery, D.L.2    Larkin, C.3    Huang, J.T.4    Hiom, K.5
  • 116
    • 80052567822 scopus 로고    scopus 로고
    • BRCA1 tumour suppression occurs via heterochromatin-mediated silencing
    • Zhu, Q. et al. BRCA1 tumour suppression occurs via heterochromatin-mediated silencing. Nature 477, 179-184 (2011).
    • (2011) Nature , vol.477 , pp. 179-184
    • Zhu, Q.1
  • 117
    • 0042317328 scopus 로고    scopus 로고
    • The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin
    • Wu-Baer, F., Lagrazon, K., Yuan, W. & Baer, R. The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J. Biol. Chem. 278, 34743-34746 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 34743-34746
    • Wu-Baer, F.1    Lagrazon, K.2    Yuan, W.3    Baer, R.4
  • 118
    • 84950294519 scopus 로고    scopus 로고
    • A mechanism for the suppression of homologous recombination in G1 cells
    • Orthwein, A. et al. A mechanism for the suppression of homologous recombination in G1 cells. Nature 528, 422-426 (2015). Reveals that homologous recombination is suppressed in the G1 phase by CRL3KEAP1-mediated ubiquitylation of PALB2, preventing its binding to BRCA2.
    • (2015) Nature , vol.528 , pp. 422-426
    • Orthwein, A.1
  • 119
    • 72449163470 scopus 로고    scopus 로고
    • The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
    • Morris, J. R. et al. The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress. Nature 462, 886-890 (2009).
    • (2009) Nature , vol.462 , pp. 886-890
    • Morris, J.R.1
  • 120
    • 72449175818 scopus 로고    scopus 로고
    • Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks
    • Galanty, Y. et al. Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks. Nature 462, 935-939 (2009).
    • (2009) Nature , vol.462 , pp. 935-939
    • Galanty, Y.1
  • 121
    • 84861941745 scopus 로고    scopus 로고
    • DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger
    • Danielsen, J. R. et al. DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger. J. Cell Biol. 197, 179-187 (2012).
    • (2012) J. Cell Biol , vol.197 , pp. 179-187
    • Danielsen, J.R.1
  • 122
    • 84861784690 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage
    • Yin, Y. et al. SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage. Genes Dev. 26, 1196-1208 (2012).
    • (2012) Genes Dev , vol.26 , pp. 1196-1208
    • Yin, Y.1
  • 123
    • 84863846456 scopus 로고    scopus 로고
    • Sumoylation of MDC1 is important for proper DNA damage response
    • Luo, K., Zhang, H., Wang, L., Yuan, J. & Lou, Z. Sumoylation of MDC1 is important for proper DNA damage response. EMBO J. 31, 3008-3019 (2012).
    • (2012) EMBO J , vol.31 , pp. 3008-3019
    • Luo, K.1    Zhang, H.2    Wang, L.3    Yuan, J.4    Lou, Z.5
  • 124
    • 84863198650 scopus 로고    scopus 로고
    • CBX4-mediated SUMO modification regulates BMI1 recruitment at sites of DNA damage
    • Ismail, I. H. et al. CBX4-mediated SUMO modification regulates BMI1 recruitment at sites of DNA damage. Nucleic Acids Res. 40, 5497-5510 (2012).
    • (2012) Nucleic Acids Res , vol.40 , pp. 5497-5510
    • Ismail, I.H.1
  • 125
    • 34548104404 scopus 로고    scopus 로고
    • RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation
    • Yan, J., Yang, X. P., Kim, Y. S., Joo, J. H. & Jetten, A. M. RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation. Biochem. Biophys. Res. Commun. 362, 132-138 (2007).
    • (2007) Biochem. Biophys. Res. Commun , vol.362 , pp. 132-138
    • Yan, J.1    Yang, X.P.2    Kim, Y.S.3    Joo, J.H.4    Jetten, A.M.5
  • 126
    • 84863659709 scopus 로고    scopus 로고
    • Scc1 sumoylation by Mms21 promotes sister chromatid recombination through counteracting Wapl
    • Wu, N. et al. Scc1 sumoylation by Mms21 promotes sister chromatid recombination through counteracting Wapl. Genes Dev. 26, 1473-1485 (2012).
    • (2012) Genes Dev , vol.26 , pp. 1473-1485
    • Wu, N.1
  • 127
    • 84946099080 scopus 로고    scopus 로고
    • NSMCE2 suppresses cancer and aging in mice independently of its SUMO ligase activity
    • Jacome, A. et al. NSMCE2 suppresses cancer and aging in mice independently of its SUMO ligase activity. EMBO J. 34, 2604-2619 (2015).
    • (2015) EMBO J , vol.34 , pp. 2604-2619
    • Jacome, A.1
  • 128
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • Psakhye, I. & Jentsch, S. Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell 151, 807-820 (2012). Describes the principle of SUMO group modification in DSB repair.
    • (2012) Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 129
    • 73949087271 scopus 로고    scopus 로고
    • SUMO modification regulates BLM and RAD51 interaction at damaged replication forks
    • Ouyang, K. J. et al. SUMO modification regulates BLM and RAD51 interaction at damaged replication forks. PLoS Biol. 7, e1000252 (2009).
    • (2009) PLoS Biol , vol.7
    • Ouyang, K.J.1
  • 130
    • 77955475870 scopus 로고    scopus 로고
    • Regulation of DNA repair through deSUMOylation and SUMOylation of replication protein A complex
    • Dou, H., Huang, C., Singh, M., Carpenter, P. B. & Yeh, E. T. Regulation of DNA repair through deSUMOylation and SUMOylation of replication protein A complex. Mol. Cell 39, 333-345 (2010).
    • (2010) Mol. Cell , vol.39 , pp. 333-345
    • Dou, H.1    Huang, C.2    Singh, M.3    Carpenter, P.B.4    Yeh, E.T.5
  • 131
    • 84887038983 scopus 로고    scopus 로고
    • The deSUMOylase SENP7 promotes chromatin relaxation for homologous recombination DNA repair
    • Garvin, A. J. et al. The deSUMOylase SENP7 promotes chromatin relaxation for homologous recombination DNA repair. EMBO Rep. 14, 975-983 (2013).
    • (2013) EMBO Rep , vol.14 , pp. 975-983
    • Garvin, A.J.1
  • 132
    • 36749009119 scopus 로고    scopus 로고
    • PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing
    • Ivanov, A. V. et al. PHD domain-mediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing. Mol. Cell 28, 823-837 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 823-837
    • Ivanov, A.V.1
  • 133
    • 79960055393 scopus 로고    scopus 로고
    • KAP-1 phosphorylation regulates CHD3 nucleosome remodeling during the DNA double-strand break response
    • Goodarzi, A. A., Kurka, T. & Jeggo, P. A. KAP-1 phosphorylation regulates CHD3 nucleosome remodeling during the DNA double-strand break response. Nat. Struct. Mol. Biol. 18, 831-839 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 831-839
    • Goodarzi, A.A.1    Kurka, T.2    Jeggo, P.A.3
  • 134
    • 75949122330 scopus 로고    scopus 로고
    • 53BP1-dependent robust localized KAP-1 phosphorylation is essential for heterochromatic DNA double-strand break repair
    • Noon, A. T. et al. 53BP1-dependent robust localized KAP-1 phosphorylation is essential for heterochromatic DNA double-strand break repair. Nat. Cell Biol. 12, 177-184 (2010).
    • (2010) Nat. Cell Biol , vol.12 , pp. 177-184
    • Noon, A.T.1
  • 135
    • 84880032059 scopus 로고    scopus 로고
    • RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response
    • Poulsen, S. L. et al. RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response. J. Cell Biol. 201, 797-807 (2013).
    • (2013) J. Cell Biol , vol.201 , pp. 797-807
    • Poulsen, S.L.1
  • 136
    • 84876849263 scopus 로고    scopus 로고
    • RNF111-dependent neddylation activates DNA damage-induced ubiquitination
    • Ma, T. et al. RNF111-dependent neddylation activates DNA damage-induced ubiquitination. Mol. Cell 49, 897-907 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 897-907
    • Ma, T.1
  • 137
    • 84920415516 scopus 로고    scopus 로고
    • Ubiquitin-SUMO circuitry controls activated Fanconi anemia ID complex dosage in response to DNA damage
    • Gibbs-Seymour, I. et al. Ubiquitin-SUMO circuitry controls activated Fanconi anemia ID complex dosage in response to DNA damage. Mol. Cell 57, 150-164 (2015).
    • (2015) Mol. Cell , vol.57 , pp. 150-164
    • Gibbs-Seymour, I.1
  • 139
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham, M. H. et al. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat. Cell Biol. 10, 538-546 (2008).
    • (2008) Nat. Cell Biol , vol.10 , pp. 538-546
    • Tatham, M.H.1
  • 140
    • 84870760201 scopus 로고    scopus 로고
    • RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage
    • Guzzo, C. M. et al. RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage. Sci. Signal. 5, ra88 (2012).
    • (2012) Sci. Signal , vol.5 , pp. ra88
    • Guzzo, C.M.1
  • 141
    • 84864076551 scopus 로고    scopus 로고
    • Rap80 protein recruitment to DNA double-strand breaks requires binding to both small ubiquitin-like modifier (SUMO) and ubiquitin conjugates
    • Hu, X., Paul, A. & Wang, B. Rap80 protein recruitment to DNA double-strand breaks requires binding to both small ubiquitin-like modifier (SUMO) and ubiquitin conjugates. J. Biol. Chem. 287, 25510-25519 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 25510-25519
    • Hu, X.1    Paul, A.2    Wang, B.3
  • 142
    • 84900790137 scopus 로고    scopus 로고
    • RNF168-mediated H2A neddylation antagonizes ubiquitylation of H2A and regulates DNA damage repair
    • Li, T., Guan, J., Huang, Z., Hu, X. & Zheng, X. RNF168-mediated H2A neddylation antagonizes ubiquitylation of H2A and regulates DNA damage repair. J. Cell Sci. 127, 2238-2248 (2014).
    • (2014) J. Cell Sci , vol.127 , pp. 2238-2248
    • Li, T.1    Guan, J.2    Huang, Z.3    Hu, X.4    Zheng, X.5
  • 143
    • 84862908377 scopus 로고    scopus 로고
    • Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes
    • Hjerpe, R. et al. Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes. Biochem. J. 441, 927-936 (2012).
    • (2012) Biochem. J , vol.441 , pp. 927-936
    • Hjerpe, R.1
  • 144
    • 84863507629 scopus 로고    scopus 로고
    • NEDD8 overexpression results in neddylation of ubiquitin substrates by the ubiquitin pathway
    • Hjerpe, R., Thomas, Y. & Kurz, T. NEDD8 overexpression results in neddylation of ubiquitin substrates by the ubiquitin pathway. J. Mol. Biol. 421, 27-29 (2012).
    • (2012) J. Mol. Biol , vol.421 , pp. 27-29
    • Hjerpe, R.1    Thomas, Y.2    Kurz, T.3
  • 146
    • 84933673434 scopus 로고    scopus 로고
    • Neddylation promotes ubiquitylation and release of Ku from DNA-damage sites
    • Brown, J. S. et al. Neddylation promotes ubiquitylation and release of Ku from DNA-damage sites. Cell Rep. 11, 704-714 (2015).
    • (2015) Cell Rep , vol.11 , pp. 704-714
    • Brown, J.S.1
  • 147
    • 84903124095 scopus 로고    scopus 로고
    • Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair
    • Zhao, Y., Brickner, J. R., Majid, M. C. & Mosammaparast, N. Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair. Trends Cell Biol. 24, 426-434 (2014).
    • (2014) Trends Cell Biol , vol.24 , pp. 426-434
    • Zhao, Y.1    Brickner, J.R.2    Majid, M.C.3    Mosammaparast, N.4
  • 148
    • 77957738825 scopus 로고    scopus 로고
    • The p400 ATPase regulates nucleosome stability and chromatin ubiquitination during DNA repair
    • Xu, Y. et al. The p400 ATPase regulates nucleosome stability and chromatin ubiquitination during DNA repair. J. Cell Biol. 191, 31-43 (2010).
    • (2010) J. Cell Biol , vol.191 , pp. 31-43
    • Xu, Y.1
  • 149
    • 84865688579 scopus 로고    scopus 로고
    • Cancer treatment according to BRCA1 and BRCA2 mutations
    • Maxwell, K. N. & Domchek, S. M. Cancer treatment according to BRCA1 and BRCA2 mutations. Nat. Rev. Clin. Oncol. 9, 520-528 (2012).
    • (2012) Nat. Rev. Clin. Oncol , vol.9 , pp. 520-528
    • Maxwell, K.N.1    Domchek, S.M.2
  • 150
    • 36749029369 scopus 로고    scopus 로고
    • RIDDLE immunodeficiency syndrome is linked to defects in 53BP1-mediated DNA damage signaling
    • Stewart, G. S. et al. RIDDLE immunodeficiency syndrome is linked to defects in 53BP1-mediated DNA damage signaling. Proc. Natl Acad. Sci. USA 104, 16910-16915 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16910-16915
    • Stewart, G.S.1
  • 151
    • 80051717220 scopus 로고    scopus 로고
    • Homozygous deficiency of ubiquitin-ligase ring-finger protein RNF168 mimics the radiosensitivity syndrome of ataxia-telangiectasia
    • Devgan, S. S. et al. Homozygous deficiency of ubiquitin-ligase ring-finger protein RNF168 mimics the radiosensitivity syndrome of ataxia-telangiectasia. Cell Death Differ. 18, 1500-1506 (2011). References 36 and 151 describe two independent cases of patients with biallelic mutations in RNF168, providing direct evidence that ubiquitin-mediated recruitment of repair factors to DSB sites is crucial for human health.
    • (2011) Cell Death Differ , vol.18 , pp. 1500-1506
    • Devgan, S.S.1
  • 152
    • 77649338569 scopus 로고    scopus 로고
    • A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses
    • Lilley, C. E. et al. A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses. EMBO J. 29, 943-955 (2010).
    • (2010) EMBO J , vol.29 , pp. 943-955
    • Lilley, C.E.1
  • 153
    • 84859731169 scopus 로고    scopus 로고
    • Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: Viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain
    • Chaurushiya, M. S. et al. Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain. Mol. Cell 46, 79-90 (2012).
    • (2012) Mol. Cell , vol.46 , pp. 79-90
    • Chaurushiya, M.S.1
  • 154
    • 84873704658 scopus 로고    scopus 로고
    • RNF4 is required for DNA double-strand break repair in vivo
    • Vyas, R. et al. RNF4 is required for DNA double-strand break repair in vivo. Cell Death Differ. 20, 490-502 (2013).
    • (2013) Cell Death Differ , vol.20 , pp. 490-502
    • Vyas, R.1
  • 155
    • 77952294873 scopus 로고    scopus 로고
    • Class switching and meiotic defects in mice lacking the E3 ubiquitin ligase RNF8
    • Santos, M. A. et al. Class switching and meiotic defects in mice lacking the E3 ubiquitin ligase RNF8. J. Exp. Med. 207, 973-981 (2010).
    • (2010) J. Exp. Med , vol.207 , pp. 973-981
    • Santos, M.A.1
  • 156
    • 77952318450 scopus 로고    scopus 로고
    • Rnf8 deficiency impairs class switch recombination, spermatogenesis, and genomic integrity and predisposes for cancer
    • Li, L. et al. Rnf8 deficiency impairs class switch recombination, spermatogenesis, and genomic integrity and predisposes for cancer. J. Exp. Med. 207, 983-997 (2010).
    • (2010) J. Exp. Med , vol.207 , pp. 983-997
    • Li, L.1
  • 157
    • 79955627875 scopus 로고    scopus 로고
    • Genomic instability, defective spermatogenesis, immunodeficiency, and cancer in a mouse model of the RIDDLE syndrome
    • Bohgaki, T. et al. Genomic instability, defective spermatogenesis, immunodeficiency, and cancer in a mouse model of the RIDDLE syndrome. PLoS Genet. 7, e1001381 (2011).
    • (2011) PLoS Genet , vol.7
    • Bohgaki, T.1
  • 158
    • 2542463148 scopus 로고    scopus 로고
    • 53BP1 is required for class switch recombination
    • Ward, I. M. et al. 53BP1 is required for class switch recombination. J. Cell Biol. 165, 459-464 (2004).
    • (2004) J. Cell Biol , vol.165 , pp. 459-464
    • Ward, I.M.1
  • 159
    • 2442707746 scopus 로고    scopus 로고
    • 53BP1 links DNA damage-response pathways to immunoglobulin heavy chain class-switch recombination
    • Manis, J. P. et al. 53BP1 links DNA damage-response pathways to immunoglobulin heavy chain class-switch recombination. Nat. Immunol. 5, 481-487 (2004).
    • (2004) Nat. Immunol , vol.5 , pp. 481-487
    • Manis, J.P.1
  • 160
    • 17244373777 scopus 로고    scopus 로고
    • Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
    • Farmer, H. et al. Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy. Nature 434, 917-921 (2005).
    • (2005) Nature , vol.434 , pp. 917-921
    • Farmer, H.1
  • 161
    • 17244375049 scopus 로고    scopus 로고
    • Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
    • Bryant, H. E. et al. Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase. Nature 434, 913-917 (2005).
    • (2005) Nature , vol.434 , pp. 913-917
    • Bryant, H.E.1
  • 162
    • 84922393807 scopus 로고    scopus 로고
    • Ubiquitination in disease pathogenesis and treatment
    • Popovic, D., Vucic, D. & Dikic, I. Ubiquitination in disease pathogenesis and treatment. Nat. Med. 20, 1242-1253 (2014).
    • (2014) Nat. Med , vol.20 , pp. 1242-1253
    • Popovic, D.1    Vucic, D.2    Dikic, I.3
  • 163
    • 84904261166 scopus 로고    scopus 로고
    • Targeting neddylation pathways to inactivate cullin-RING ligases for anticancer therapy
    • Zhao, Y., Morgan, M. A. & Sun, Y. Targeting neddylation pathways to inactivate cullin-RING ligases for anticancer therapy. Antioxid. Redox Signal. 21, 2383-2400 (2014).
    • (2014) Antioxid. Redox Signal , vol.21 , pp. 2383-2400
    • Zhao, Y.1    Morgan, M.A.2    Sun, Y.3
  • 164
    • 84883196231 scopus 로고    scopus 로고
    • Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death
    • Magnaghi, P. et al. Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death. Nat. Chem. Biol. 9, 548-556 (2013).
    • (2013) Nat. Chem. Biol , vol.9 , pp. 548-556
    • Magnaghi, P.1
  • 165
    • 84867101049 scopus 로고    scopus 로고
    • Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass
    • Povlsen, L. K. et al. Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Nat. Cell Biol. 14, 1089-1098 (2012).
    • (2012) Nat. Cell Biol , vol.14 , pp. 1089-1098
    • Povlsen, L.K.1
  • 167
    • 84873734105 scopus 로고    scopus 로고
    • RNA-guided human genome engineering via Cas9
    • Mali, P. et al. RNA-guided human genome engineering via Cas9. Science 339, 823-826 (2013).
    • (2013) Science , vol.339 , pp. 823-826
    • Mali, P.1
  • 168
    • 84873729095 scopus 로고    scopus 로고
    • Multiplex genome engineering using CRISPR/Cas systems
    • Cong, L. et al. Multiplex genome engineering using CRISPR/Cas systems. Science 339, 819-823 (2013).
    • (2013) Science , vol.339 , pp. 819-823
    • Cong, L.1
  • 169
    • 84892765883 scopus 로고    scopus 로고
    • Genome-scale CRISPR-Cas9 knockout screening in human cells
    • Shalem, O. et al. Genome-scale CRISPR-Cas9 knockout screening in human cells. Science 343, 84-87 (2014).
    • (2014) Science , vol.343 , pp. 84-87
    • Shalem, O.1
  • 170
    • 84892749369 scopus 로고    scopus 로고
    • Genetic screens in human cells using the CRISPR-Cas9 system
    • Wang, T., Wei, J. J., Sabatini, D. M. & Lander, E. S. Genetic screens in human cells using the CRISPR-Cas9 system. Science 343, 80-84 (2014).
    • (2014) Science , vol.343 , pp. 80-84
    • Wang, T.1    Wei, J.J.2    Sabatini, D.M.3    Lander, E.S.4
  • 171
    • 84925949741 scopus 로고    scopus 로고
    • Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest)
    • Hospenthal, M. K., Mevissen, T. E. & Komander, D. Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest). Nat. Protoc. 10, 349-361 (2015).
    • (2015) Nat. Protoc , vol.10 , pp. 349-361
    • Hospenthal, M.K.1    Mevissen, T.E.2    Komander, D.3


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