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Volumn 21, Issue 4, 2014, Pages 317-324

Two-way communications between ubiquitin-like modifiers and DNA

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; DNA; FANCONI ANEMIA PROTEIN; INTERFERON REGULATORY FACTOR 1; MULTIPROTEIN COMPLEX; SUMO PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; ADENOSINE TRIPHOSPHATASE; BMI1 PROTEIN; HISTONE H2A; POLYUBIQUITIN; PROTEIN INHIBITOR OF ACTIVATED STAT; RAP1 PROTEIN; REPLICATION FACTOR A; RNA POLYMERASE II; UBIQUITIN PROTEIN LIGASE;

EID: 84898745559     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2805     Document Type: Review
Times cited : (36)

References (127)
  • 1
    • 84878944582 scopus 로고    scopus 로고
    • SUMOylation a regulatory protein modification in health and disease
    • Flotho, A. & Melchior, F. SUMOylation: A regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357-385 (2013
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 2
    • 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
  • 3
  • 4
    • 77953915005 scopus 로고    scopus 로고
    • Ubiquitin signalling in DNA replication and repair
    • Ulrich, H.D. & Walden, H. Ubiquitin signalling in DNA replication and repair. Nat. Rev. Mol. Cell Biol. 11, 479-489 (2010
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 479-489
    • Ulrich, H.D.1    Walden, H.2
  • 5
    • 84861869979 scopus 로고    scopus 로고
    • Ubiquitin and proteasomes in transcription
    • Geng, F., Wenzel, S. & Tansey, W.P. Ubiquitin and proteasomes in transcription. Annu. Rev. Biochem. 81, 177-201 (2012
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 177-201
    • Geng, F.1    Wenzel, S.2    Tansey, W.P.3
  • 6
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • Gill, G. SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms? Genes Dev. 18, 2046-2059 (2004
    • (2004) Genes Dev , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 7
    • 1942437991 scopus 로고    scopus 로고
    • SUMO a regulator of gene expression and genome integrity
    • Müller, S., Ledl, A. & Schmidt, D. SUMO: A regulator of gene expression and genome integrity. Oncogene 23, 1998-2008 (2004
    • (2004) Oncogene , vol.23 , pp. 1998-2008
    • Müller, S.1    Ledl, A.2    Schmidt, D.3
  • 8
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and SUMO modifications in DNA repair
    • Bergink, S. & Jentsch, S. Principles of ubiquitin and SUMO modifications in DNA repair. Nature 458, 461-467 (2009
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 9
    • 0034161452 scopus 로고    scopus 로고
    • SAP a putative DNA-binding motif involved in chromosomal organization
    • Aravind, L. & Koonin, E.V. SAP: A putative DNA-binding motif involved in chromosomal organization. Trends Biochem. Sci. 25, 112-114 (2000
    • (2000) Trends Biochem. Sci , vol.25 , pp. 112-114
    • Aravind, L.1    Koonin, E.V.2
  • 10
    • 37749037140 scopus 로고    scopus 로고
    • PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription
    • Palvimo, J.J. PIAS proteins as regulators of small ubiquitin-related modifier (SUMO) modifications and transcription. Biochem. Soc. Trans. 35, 1405-1408 (2007
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 1405-1408
    • Palvimo, J.J.1
  • 11
    • 66149091527 scopus 로고    scopus 로고
    • Solution structures and DNA binding properties of the N-Terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa
    • Suzuki, R. et al. Solution structures and DNA binding properties of the N-Terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa. Proteins 75, 336-347 (2009
    • (2009) Proteins , vol.75 , pp. 336-347
    • Suzuki, R.1
  • 12
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G.L., Pyrowolakis, G. & Jentsch, S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141 (2002
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 13
    • 57349113038 scopus 로고    scopus 로고
    • Cooperation of replication protein A with the ubiquitin ligase Rad18 in DNA damage bypass
    • Huttner, D. & Ulrich, H.D. Cooperation of replication protein A with the ubiquitin ligase Rad18 in DNA damage bypass. Cell Cycle 7, 3629-3633 (2008
    • (2008) Cell Cycle , vol.7 , pp. 3629-3633
    • Huttner, D.1    Ulrich, H.D.2
  • 14
    • 33845933389 scopus 로고    scopus 로고
    • Replication-dependent and-independent responses of RAD18 to DNA damage in human cells
    • Nakajima, S. et al. Replication-dependent and-independent responses of RAD18 to DNA damage in human cells. J. Biol. Chem. 281, 34687-34695 (2006
    • (2006) J. Biol. Chem , vol.281 , pp. 34687-34695
    • Nakajima, S.1
  • 15
    • 34848877881 scopus 로고    scopus 로고
    • Functional characterization of Rad18 domains for Rad6, ubiquitin, DNA binding and PCNA modification
    • Notenboom, V. et al. Functional characterization of Rad18 domains for Rad6, ubiquitin, DNA binding and PCNA modification. Nucleic Acids Res. 35, 5819-5830 (2007
    • (2007) Nucleic Acids Res , vol.35 , pp. 5819-5830
    • Notenboom, V.1
  • 16
    • 41149165416 scopus 로고    scopus 로고
    • Recognition of forked and single-stranded DNA structures by human RAD18 complexed with RAD6B protein triggers its recruitment to stalled replication forks
    • Tsuji, Y. et al. Recognition of forked and single-stranded DNA structures by human RAD18 complexed with RAD6B protein triggers its recruitment to stalled replication forks. Genes Cells 13, 343-354 (2008
    • (2008) Genes Cells , vol.13 , pp. 343-354
    • Tsuji, Y.1
  • 18
    • 0029157378 scopus 로고
    • Evolution of the SNF2 family of proteins: Subfamilies with distinct sequences and functions
    • Eisen, J.A., Sweder, K.S. & Hanawalt, P.C. Evolution of the SNF2 family of proteins: Subfamilies with distinct sequences and functions. Nucleic Acids Res. 23, 2715-2723 (1995
    • (1995) Nucleic Acids Res , vol.23 , pp. 2715-2723
    • Eisen, J.A.1    Sweder, K.S.2    Hanawalt, P.C.3
  • 19
    • 12044250532 scopus 로고
    • The RAD6 DNA repair pathway in Saccharomyces cerevisiae: What does it do, and how does it do it?
    • Lawrence, C. The RAD6 DNA repair pathway in Saccharomyces cerevisiae: What does it do, and how does it do it? BioEssays 16, 253-258 (1994
    • (1994) BioEssays , vol.16 , pp. 253-258
    • Lawrence, C.1
  • 20
    • 71349084952 scopus 로고    scopus 로고
    • Mechanistic analysis of PCNA poly-ubiquitylation by the ubiquitin protein ligases Rad18 and Rad5
    • Parker, J.L. & Ulrich, H.D. Mechanistic analysis of PCNA poly-ubiquitylation by the ubiquitin protein ligases Rad18 and Rad5. EMBO J. 28, 3657-3666 (2009
    • (2009) EMBO J. , vol.28 , pp. 3657-3666
    • Parker, J.L.1    Ulrich, H.D.2
  • 21
    • 29444454665 scopus 로고    scopus 로고
    • Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases ? and REV1
    • Garg, P. & Burgers, P.M. Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases ? and REV1. Proc. Natl. Acad. Sci. USA 102, 18361-18366 (2005
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18361-18366
    • Garg, P.1    Burgers, P.M.2
  • 22
    • 33645711927 scopus 로고    scopus 로고
    • The HIRAN domain and recruitment of chromatin remodeling and repair activities to damaged DNA
    • Iyer, L.M., Babu, M.M. & Aravind, L. The HIRAN domain and recruitment of chromatin remodeling and repair activities to damaged DNA. Cell Cycle 5, 775-782 (2006
    • (2006) Cell Cycle , vol.5 , pp. 775-782
    • Iyer, L.M.1    Babu, M.M.2    Aravind, L.3
  • 23
    • 75149143176 scopus 로고    scopus 로고
    • Role of double-stranded DNA translocase activity of human HLTF in replication of damaged DNA
    • Blastyák, A., Hajdu, I., Unk, I. & Haracska, L. Role of double-stranded DNA translocase activity of human HLTF in replication of damaged DNA. Mol. Cell. Biol. 30, 684-693 (2010
    • (2010) Mol. Cell. Biol , vol.30 , pp. 684-693
    • Blastyák, A.1    Hajdu, I.2    Unk, I.3    Haracska, L.4
  • 24
    • 35148847451 scopus 로고    scopus 로고
    • Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression
    • Blastyák, A. et al. Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression. Mol. Cell 28, 167-175 (2007
    • (2007) Mol. Cell , vol.28 , pp. 167-175
    • Blastyák, A.1
  • 26
    • 36348977099 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolytic control of SUMO conjugates
    • Uzunova, K. et al. Ubiquitin-dependent proteolytic control of SUMO conjugates. J. Biol. Chem. 282, 34167-34175 (2007
    • (2007) J. Biol. Chem , vol.282 , pp. 34167-34175
    • Uzunova, K.1
  • 27
    • 84875472600 scopus 로고    scopus 로고
    • End-joining inhibition at telomeres requires the translocase and polySUMO-dependent ubiquitin ligase Uls1
    • Lescasse, R., Pobiega, S., Callebaut, I. & Marcand, S. End-joining inhibition at telomeres requires the translocase and polySUMO-dependent ubiquitin ligase Uls1. EMBO J. 32, 805-815 (2013
    • (2013) EMBO J. , vol.32 , pp. 805-815
    • Lescasse, R.1    Pobiega, S.2    Callebaut, I.3    Marcand, S.4
  • 28
    • 0035968277 scopus 로고    scopus 로고
    • The RING finger protein SNURF is a bifunctional protein possessing DNA binding activity
    • Häkli, M., Karvonen, U., Janne, O.A. & Palvimo, J.J. The RING finger protein SNURF is a bifunctional protein possessing DNA binding activity. J. Biol. Chem. 276, 23653-23660 (2001
    • (2001) J. Biol. Chem , vol.276 , pp. 23653-23660
    • Häkli, M.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 29
    • 70349316411 scopus 로고    scopus 로고
    • Role of polycomb proteins Ring1A and Ring1B in the epigenetic regulation of gene expression
    • Vidal, M. Role of polycomb proteins Ring1A and Ring1B in the epigenetic regulation of gene expression. Int. J. Dev. Biol. 53, 355-370 (2009
    • (2009) Int. J. Dev. Biol , vol.53 , pp. 355-370
    • Vidal, M.1
  • 30
    • 80155198826 scopus 로고    scopus 로고
    • Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex
    • Bentley, M.L. et al. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. EMBO J. 30, 3285-3297 (2011
    • (2011) EMBO J. , vol.30 , pp. 3285-3297
    • Bentley, M.L.1
  • 31
    • 80052743035 scopus 로고    scopus 로고
    • Detecting UV-lesions in the genome: The modular CRL4 ubiquitin ligase does it best!.
    • Scrima, A. et al. Detecting UV-lesions in the genome: The modular CRL4 ubiquitin ligase does it best!. FEBS Lett. 585, 2818-2825 (2011
    • (2011) FEBS Lett , vol.585 , pp. 2818-2825
    • Scrima, A.1
  • 32
    • 75749144248 scopus 로고    scopus 로고
    • Regulation of damage recognition in mammalian global genomic nucleotide excision repair
    • Sugasawa, K. Regulation of damage recognition in mammalian global genomic nucleotide excision repair. Mutat. Res. 685, 29-37 (2010
    • (2010) Mutat. Res , vol.685 , pp. 29-37
    • Sugasawa, K.1
  • 33
    • 81855227619 scopus 로고    scopus 로고
    • The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation
    • Fischer, E.S. et al. The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation. Cell 147, 1024-1039 (2011
    • (2011) Cell , vol.147 , pp. 1024-1039
    • Fischer, E.S.1
  • 34
    • 84867376482 scopus 로고    scopus 로고
    • Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair
    • Yeh, J.I. et al. Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair. Proc. Natl. Acad. Sci. USA 109, E2737-E2746 (2012
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Yeh, J.I.1
  • 35
    • 80052393142 scopus 로고    scopus 로고
    • The Smc5/6 complex: More than repair? Cold Spring Harb
    • Kegel, A. & Sjogren, C. The Smc5/6 complex: More than repair? Cold Spring Harb. Symp. Quant. Biol. 75, 179-187 (2010
    • (2010) Symp. Quant. Biol , vol.75 , pp. 179-187
    • Kegel, A.1    Sjogren, C.2
  • 36
    • 84862899536 scopus 로고    scopus 로고
    • The Smc complexes in DNA damage response
    • Wu, N. & Yu, H. The Smc complexes in DNA damage response. Cell Biosci. 2, 5 (2012
    • (2012) Cell Biosci , vol.2 , pp. 5
    • Wu, N.1    Yu, H.2
  • 37
    • 11144324990 scopus 로고    scopus 로고
    • Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage
    • Andrews, E.A. et al. Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage. Mol. Cell. Biol. 25, 185-196 (2005
    • (2005) Mol. Cell. Biol , vol.25 , pp. 185-196
    • Andrews, E.A.1
  • 38
    • 69949088463 scopus 로고    scopus 로고
    • Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex
    • Duan, X. et al. Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex. Mol. Cell 35, 657-668 (2009
    • (2009) Mol. Cell , vol.35 , pp. 657-668
    • Duan, X.1
  • 39
    • 23344442009 scopus 로고    scopus 로고
    • Human MMS21/NSE2 is a SUMO ligase required for DNA repair
    • Potts, P.R. & Yu, H. Human MMS21/NSE2 is a SUMO ligase required for DNA repair. Mol. Cell. Biol. 25, 7021-7032 (2005
    • (2005) Mol. Cell. Biol , vol.25 , pp. 7021-7032
    • Potts, P.R.1    Yu, H.2
  • 40
    • 16344370926 scopus 로고    scopus 로고
    • A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization
    • Zhao, X. & Blobel, G. A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl. Acad. Sci. USA 102, 4777-4782 (2005
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4777-4782
    • Zhao, X.1    Blobel, G.2
  • 41
    • 77956936946 scopus 로고    scopus 로고
    • MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases
    • Doyle, J.M., Gao, J., Wang, J., Yang, M. & Potts, P.R. MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases. Mol. Cell 39, 963-974 (2010
    • (2010) Mol. Cell , vol.39 , pp. 963-974
    • Doyle, J.M.1    Gao, J.2    Wang, J.3    Yang, M.4    Potts, P.R.5
  • 42
    • 84863670930 scopus 로고    scopus 로고
    • Regulation of DNA cross-link repair by the Fanconi anemia/BRCA pathway
    • Kim, H. & D'Andrea, A.D. Regulation of DNA cross-link repair by the Fanconi anemia/BRCA pathway. Genes Dev. 26, 1393-1408 (2012
    • (2012) Genes Dev , vol.26 , pp. 1393-1408
    • Kim, H.1    D'Andrea, A.D.2
  • 43
    • 84872578210 scopus 로고    scopus 로고
    • Fanconi anaemia and the repair of Watson and Crick DNA crosslinks
    • Kottemann, M.C. & Smogorzewska, A. Fanconi anaemia and the repair of Watson and Crick DNA crosslinks. Nature 493, 356-363 (2013
    • (2013) Nature , vol.493 , pp. 356-363
    • Kottemann, M.C.1    Smogorzewska, A.2
  • 44
    • 84883487898 scopus 로고    scopus 로고
    • Architecture and DNA recognition elements of the Fanconi anemia FANCM-FAAP24 complex
    • Coulthard, R. et al. Architecture and DNA recognition elements of the Fanconi anemia FANCM-FAAP24 complex. Structure 21, 1648-1658 (2013
    • (2013) Structure , vol.21 , pp. 1648-1658
    • Coulthard, R.1
  • 45
    • 84860263013 scopus 로고    scopus 로고
    • The structure of the FANCM-MHF complex reveals physical features for functional assembly
    • Tao, Y. et al. The structure of the FANCM-MHF complex reveals physical features for functional assembly. Nat. Commun. 3, 782 (2012
    • (2012) Nat. Commun , vol.3 , pp. 782
    • Tao, Y.1
  • 46
    • 70450265298 scopus 로고    scopus 로고
    • The amino-Terminal TPR domain of Dia2 tethers SCFDia2 to the replisome progression complex
    • Morohashi, H., Maculins, T. & Labib, K. The amino-Terminal TPR domain of Dia2 tethers SCFDia2 to the replisome progression complex. Curr. Biol. 19, 1943-1949 (2009
    • (2009) Curr. Biol , vol.19 , pp. 1943-1949
    • Morohashi, H.1    Maculins, T.2    Labib, K.3
  • 47
    • 71249158149 scopus 로고    scopus 로고
    • SCFDia2 regulates DNA replication forks during S-phase in budding yeast
    • Mimura, S., Komata, M., Kishi, T., Shirahige, K. & Kamura, T. SCFDia2 regulates DNA replication forks during S-phase in budding yeast. EMBO J. 28, 3693-3705 (2009
    • (2009) EMBO J. , vol.28 , pp. 3693-3705
    • Mimura, S.1    Komata, M.2    Kishi, T.3    Shirahige, K.4    Kamura, T.5
  • 48
    • 79959301489 scopus 로고    scopus 로고
    • Dia2 controls transcription by mediating assembly of the RSC complex
    • Andress, E.J., Holic, R., Edelmann, M.J., Kessler, B.M. & Yu, V.P. Dia2 controls transcription by mediating assembly of the RSC complex. PLoS ONE 6, e21172 (2011
    • (2011) PLoS ONE , vol.6
    • Andress, E.J.1    Holic, R.2    Edelmann, M.J.3    Kessler, B.M.4    Yu, V.P.5
  • 49
    • 68949149115 scopus 로고    scopus 로고
    • Direct Bre1-Paf1 complex interactions and RING finger-independent Bre1-Rad6 interactions mediate histone H2B ubiquitylation in yeast
    • Kim, J. & Roeder, R.G. Direct Bre1-Paf1 complex interactions and RING finger-independent Bre1-Rad6 interactions mediate histone H2B ubiquitylation in yeast. J. Biol. Chem. 284, 20582-20592 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 20582-20592
    • Kim, J.1    Roeder, R.G.2
  • 50
    • 40649097306 scopus 로고    scopus 로고
    • Activation of ubiquitin-dependent DNA damage bypass is mediated by Replication Protein A
    • Davies, A.A., Huttner, D., Daigaku, Y., Chen, S. & Ulrich, H.D. Activation of ubiquitin-dependent DNA damage bypass is mediated by Replication Protein A. Mol. Cell 29, 625-636 (2008
    • (2008) Mol Cell , vol.29 , pp. 625-636
    • Davies, A.A.1    Huttner, D.2    Daigaku, Y.3    Chen, S.4    Ulrich, H.D.5
  • 51
    • 55849091416 scopus 로고    scopus 로고
    • Regulation of proliferating cell nuclear antigen ubiquitination in mammalian cells
    • Niimi, A. et al. Regulation of proliferating cell nuclear antigen ubiquitination in mammalian cells. Proc. Natl. Acad. Sci. USA 105, 16125-16130 (2008
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16125-16130
    • Niimi, A.1
  • 52
    • 78649492271 scopus 로고    scopus 로고
    • The ubiquitous role of ubiquitin in the DNA damage response
    • Al-Hakim, A. et al. The ubiquitous role of ubiquitin in the DNA damage response. DNA Repair (Amst.) 9, 1229-1240 (2010
    • (2010) DNA Repair (Amst , vol.9 , pp. 1229-1240
    • Al-Hakim, A.1
  • 53
    • 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
  • 54
    • 84858147489 scopus 로고    scopus 로고
    • Ubiquitin and SUMO in DNA repair at a glance
    • Ulrich, H.D. Ubiquitin and SUMO in DNA repair at a glance. J. Cell Sci. 125, 249-254 (2012
    • (2012) J. Cell Sci , vol.125 , pp. 249-254
    • Ulrich, H.D.1
  • 55
    • 84886950182 scopus 로고    scopus 로고
    • Structural mechanisms underlying signaling in the cellular response to DNA double strand breaks
    • Mermershtain, I. & Glover, J.N. Structural mechanisms underlying signaling in the cellular response to DNA double strand breaks. Mutat. Res. 750, 15-22 (2013
    • (2013) Mutat. Res , vol.750 , pp. 15-22
    • Mermershtain, I.1    Glover, J.N.2
  • 56
    • 30744465308 scopus 로고    scopus 로고
    • MDC1 maintains genomic stability by participating in the amplification of ATM-dependent DNA damage signals
    • Lou, Z. et al. MDC1 maintains genomic stability by participating in the amplification of ATM-dependent DNA damage signals. Mol. Cell 21, 187-200 (2006
    • (2006) Mol. Cell , vol.21 , pp. 187-200
    • Lou, Z.1
  • 57
  • 58
    • 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
  • 59
    • 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
  • 60
    • 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
  • 61
    • 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
  • 62
    • 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
  • 63
    • 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
  • 64
    • 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
  • 65
    • 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
  • 66
    • 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
  • 67
    • 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
  • 68
    • 34547662882 scopus 로고    scopus 로고
    • CCDC98 targets BRCA1 to DNA damage sites
    • Liu, Z., Wu, J. & Yu, X. CCDC98 targets BRCA1 to DNA damage sites. Nat. Struct. Mol. Biol. 14, 716-720 (2007
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 716-720
    • Liu, Z.1    Wu, J.2    Yu, X.3
  • 69
    • 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
  • 70
    • 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
  • 72
    • 0034694841 scopus 로고    scopus 로고
    • The BRCT regions of tumor suppressor BRCA1 and of XRCC1 show DNA end binding activity with a multimerizing feature
    • Yamane, K., Katayama, E. & Tsuruo, T. The BRCT regions of tumor suppressor BRCA1 and of XRCC1 show DNA end binding activity with a multimerizing feature. Biochem. Biophys. Res. Commun. 279, 678-684 (2000
    • (2000) Biochem. Biophys. Res. Commun , vol.279 , pp. 678-684
    • Yamane, K.1    Katayama, E.2    Tsuruo, T.3
  • 73
    • 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
  • 74
    • 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
  • 75
    • 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
  • 76
    • 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
  • 77
    • 84871206469 scopus 로고    scopus 로고
    • A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA
    • Parker, J.L. & Ulrich, H.D. A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA. Nucleic Acids Res. 40, 11380-11388 (2012
    • (2012) Nucleic Acids Res , vol.40 , pp. 11380-11388
    • Parker, J.L.1    Ulrich, H.D.2
  • 78
    • 80051525031 scopus 로고    scopus 로고
    • Mechanism of CRL4Cdt2, a PCNA-dependent E3 ubiquitin ligase
    • Havens, C.G. & Walter, J.C. Mechanism of CRL4Cdt2, a PCNA-dependent E3 ubiquitin ligase. Genes Dev. 25, 1568-1582 (2011
    • (2011) Genes Dev , vol.25 , pp. 1568-1582
    • Havens, C.G.1    Walter, J.C.2
  • 79
    • 11844273174 scopus 로고    scopus 로고
    • Replication-dependent destruction of Cdt1 limits DNA replication to a single round per cell cycle in Xenopus egg extracts
    • Arias, E.E. & Walter, J.C. Replication-dependent destruction of Cdt1 limits DNA replication to a single round per cell cycle in Xenopus egg extracts. Genes Dev. 19, 114-126 (2005
    • (2005) Genes Dev , vol.19 , pp. 114-126
    • Arias, E.E.1    Walter, J.C.2
  • 80
    • 5444274523 scopus 로고    scopus 로고
    • Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage
    • Hu, J., McCall, C.M., Ohta, T. & Xiong, Y. Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage. Nat. Cell Biol. 6, 1003-1009 (2004
    • (2004) Nat. Cell Biol , vol.6 , pp. 1003-1009
    • Hu, J.1    McCall, C.M.2    Ohta, T.3    Xiong, Y.4
  • 81
    • 3042686494 scopus 로고    scopus 로고
    • Rapid degradation of Cdt1 upon UV-induced DNA damage is mediated by SCFSkp2 complex
    • Kondo, T. et al. Rapid degradation of Cdt1 upon UV-induced DNA damage is mediated by SCFSkp2 complex. J. Biol. Chem. 279, 27315-27319 (2004
    • (2004) J. Biol. Chem , vol.279 , pp. 27315-27319
    • Kondo, T.1
  • 82
    • 30344455639 scopus 로고    scopus 로고
    • PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
    • Arias, E.E. & Walter, J.C. PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication. Nat. Cell Biol. 8, 84-90 (2006
    • (2006) Nat. Cell Biol , vol.8 , pp. 84-90
    • Arias, E.E.1    Walter, J.C.2
  • 83
    • 33645212112 scopus 로고    scopus 로고
    • An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage
    • Hu, J. & Xiong, Y. An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage. J. Biol. Chem. 281, 3753-3756 (2006
    • (2006) J. Biol. Chem , vol.281 , pp. 3753-3756
    • Hu, J.1    Xiong, Y.2
  • 84
    • 33747873322 scopus 로고    scopus 로고
    • A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1
    • Jin, J., Arias, E.E., Chen, J., Harper, J.W. & Walter, J.C. A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. Mol. Cell 23, 709-721 (2006
    • (2006) Mol. Cell , vol.23 , pp. 709-721
    • Jin, J.1    Arias, E.E.2    Chen, J.3    Harper, J.W.4    Walter, J.C.5
  • 85
    • 33646504727 scopus 로고    scopus 로고
    • PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-Terminal ubiquitination
    • Senga, T. et al. PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-Terminal ubiquitination. J. Biol. Chem. 281, 6246-6252 (2006
    • (2006) J. Biol. Chem , vol.281 , pp. 6246-6252
    • Senga, T.1
  • 86
    • 67649641658 scopus 로고    scopus 로고
    • Docking of a specialized PIP Box onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2
    • Havens, C.G. & Walter, J.C. Docking of a specialized PIP Box onto chromatin-bound PCNA creates a degron for the ubiquitin ligase CRL4Cdt2. Mol. Cell 35, 93-104 (2009
    • (2009) Mol. Cell , vol.35 , pp. 93-104
    • Havens, C.G.1    Walter, J.C.2
  • 87
    • 84859483427 scopus 로고    scopus 로고
    • Direct role for proliferating cell nuclear antigen in substrate recognition by the E3 ubiquitin ligase CRL4Cdt2
    • Havens, C.G. et al. Direct role for proliferating cell nuclear antigen in substrate recognition by the E3 ubiquitin ligase CRL4Cdt2. J. Biol. Chem. 287, 11410-11421 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 11410-11421
    • Havens, C.G.1
  • 88
    • 51949112601 scopus 로고    scopus 로고
    • The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to control replication licensing
    • Kim, Y., Starostina, N.G. & Kipreos, E.T. The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to control replication licensing. Genes Dev. 22, 2507-2519 (2008
    • (2008) Genes Dev , vol.22 , pp. 2507-2519
    • Kim, Y.1    Starostina, N.G.2    Kipreos, E.T.3
  • 89
    • 57049133181 scopus 로고    scopus 로고
    • CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation
    • Nishitani, H. et al. CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation. J. Biol. Chem. 283, 29045-29052 (2008
    • (2008) J. Biol. Chem , vol.283 , pp. 29045-29052
    • Nishitani, H.1
  • 90
    • 51949098691 scopus 로고    scopus 로고
    • PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex
    • Abbas, T. et al. PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex. Genes Dev. 22, 2496-2506 (2008
    • (2008) Genes Dev , vol.22 , pp. 2496-2506
    • Abbas, T.1
  • 91
    • 77957367739 scopus 로고    scopus 로고
    • CRL4Cdt2-mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase
    • Centore, R.C. et al. CRL4Cdt2-mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase. Mol. Cell 40, 22-33 (2010
    • (2010) Mol. Cell , vol.40 , pp. 22-33
    • Centore, R.C.1
  • 92
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and-independent mechanisms
    • Liu, C. et al. Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and-independent mechanisms. Genes Dev. 17, 1130-1140 (2003
    • (2003) Genes Dev , vol.17 , pp. 1130-1140
    • Liu, C.1
  • 93
    • 84880528179 scopus 로고    scopus 로고
    • The helicase FBH1 is tightly regulated by PCNA via CRL4Cdt2-mediated proteolysis in human cells
    • Bacquin, A. et al. The helicase FBH1 is tightly regulated by PCNA via CRL4Cdt2-mediated proteolysis in human cells. Nucleic Acids Res. 41, 6501-6513 (2013
    • (2013) Nucleic Acids Res , vol.41 , pp. 6501-6513
    • Bacquin, A.1
  • 94
    • 57049097607 scopus 로고    scopus 로고
    • Intrinsic negative cell cycle regulation provided by PIP box-And Cul4Cdt2-mediated destruction of E2f1 during S phase
    • Shibutani, S.T. et al. Intrinsic negative cell cycle regulation provided by PIP box-And Cul4Cdt2-mediated destruction of E2f1 during S phase. Dev. Cell 15, 890-900 (2008
    • (2008) Dev. Cell , vol.15 , pp. 890-900
    • Shibutani, S.T.1
  • 95
    • 57749101303 scopus 로고    scopus 로고
    • Regulated proteolysis of DNA polymerase eta during the DNA-damage response in C elegans
    • Kim, S.H. & Michael, W.M. Regulated proteolysis of DNA polymerase eta during the DNA-damage response in C elegans. Mol. Cell 32, 757-766 (2008
    • (2008) Mol. Cell , vol.32 , pp. 757-766
    • Kim, S.H.1    Michael, W.M.2
  • 97
    • 0031902872 scopus 로고    scopus 로고
    • Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing
    • Shinohara, A., Shinohara, M., Ohta, T., Matsuda, S. & Ogawa, T. Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing. Genes Cells 3, 145-156 (1998
    • (1998) Genes Cells , vol.3 , pp. 145-156
    • Shinohara, A.1    Shinohara, M.2    Ohta, T.3    Matsuda, S.4    Ogawa, T.5
  • 98
    • 33750499289 scopus 로고    scopus 로고
    • Control of Rad52 recombination activity by double-strand break-induced SUMO modification
    • Sacher, M., Pfander, B., Hoege, C. & Jentsch, S. Control of Rad52 recombination activity by double-strand break-induced SUMO modification. Nat. Cell Biol. 8, 1284-1290 (2006
    • (2006) Nat. Cell Biol , vol.8 , pp. 1284-1290
    • Sacher, M.1    Pfander, B.2    Hoege, C.3    Jentsch, S.4
  • 99
    • 34547591933 scopus 로고    scopus 로고
    • The Smc5-Smc6 complex and SUMO modification of Rad52 regulates recombinational repair at the ribosomal gene locus
    • Torres-Rosell, J. et al. The Smc5-Smc6 complex and SUMO modification of Rad52 regulates recombinational repair at the ribosomal gene locus. Nat. Cell Biol. 9, 923-931 (2007
    • (2007) Nat. Cell Biol , vol.9 , pp. 923-931
    • Torres-Rosell, J.1
  • 100
    • 77955813573 scopus 로고    scopus 로고
    • Rad52 SUMOylation affects the efficiency of the DNA repair
    • Altmannova, V. et al. Rad52 SUMOylation affects the efficiency of the DNA repair. Nucleic Acids Res. 38, 4708-4721 (2010
    • (2010) Nucleic Acids Res , vol.38 , pp. 4708-4721
    • Altmannova, V.1
  • 101
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • Papouli, E. et al. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol. Cell 19, 123-133 (2005
    • (2005) Mol. Cell , vol.19 , pp. 123-133
    • Papouli, E.1
  • 102
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • Pfander, B., Moldovan, G.L., Sacher, M., Hoege, C. & Jentsch, S. SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436, 428-433 (2005
    • (2005) Nature , vol.436 , pp. 428-433
    • Pfander, B.1    Moldovan, G.L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 103
    • 51949083815 scopus 로고    scopus 로고
    • SUMO modification of PCNA is controlled by DNA
    • Parker, J.L. et al. SUMO modification of PCNA is controlled by DNA. EMBO J. 27, 2422-2431 (2008
    • (2008) EMBO J. , vol.27 , pp. 2422-2431
    • Parker, J.L.1
  • 104
    • 38049079191 scopus 로고    scopus 로고
    • Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae
    • Windecker, H. & Ulrich, H.D. Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae. J. Mol. Biol. 376, 221-231 (2008
    • (2008) J. Mol. Biol , vol.376 , pp. 221-231
    • Windecker, H.1    Ulrich, H.D.2
  • 106
    • 84880961949 scopus 로고    scopus 로고
    • DNA-dependent SUMO modification of PARP-1
    • Zilio, N. et al. DNA-dependent SUMO modification of PARP-1. DNA Repair (Amst.) 12, 761-773 (2013
    • (2013) DNA Repair (Amst , vol.12 , pp. 761-773
    • Zilio, N.1
  • 107
    • 44949253890 scopus 로고    scopus 로고
    • Poly ADP-ribose polymerase-1: An international molecule of mystery
    • Woodhouse, B.C. & Dianov, G.L. Poly ADP-ribose polymerase-1: An international molecule of mystery. DNA Repair (Amst.) 7, 1077-1086 (2008
    • (2008) DNA Repair (Amst , vol.7 , pp. 1077-1086
    • Woodhouse, B.C.1    Dianov, G.L.2
  • 108
    • 70450255284 scopus 로고    scopus 로고
    • PARP-1 transcriptional activity is regulated by SUMOylation upon heat shock
    • Martin, N. et al. PARP-1 transcriptional activity is regulated by SUMOylation upon heat shock. EMBO J. 28, 3534-3548 (2009
    • (2009) EMBO J. , vol.28 , pp. 3534-3548
    • Martin, N.1
  • 109
    • 70350548179 scopus 로고    scopus 로고
    • SUMOylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function
    • Messner, S. et al. SUMOylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function. FASEB J. 23, 3978-3989 (2009
    • (2009) FASEB J. , vol.23 , pp. 3978-3989
    • Messner, S.1
  • 110
    • 84872414012 scopus 로고    scopus 로고
    • Ubiquitylation and degradation of elongating RNA polymerase II: The last resort
    • Wilson, M.D., Harreman, M. & Svejstrup, J.Q. Ubiquitylation and degradation of elongating RNA polymerase II: The last resort. Biochim. Biophys. Acta 1829, 151-157 (2013
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 151-157
    • Wilson, M.D.1    Harreman, M.2    Svejstrup, J.Q.3
  • 111
    • 73949101221 scopus 로고    scopus 로고
    • Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation
    • Harreman, M. et al. Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc. Natl. Acad. Sci. USA 106, 20705-20710 (2009
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20705-20710
    • Harreman, M.1
  • 112
    • 20444428382 scopus 로고    scopus 로고
    • Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest
    • Somesh, B.P. et al. Multiple mechanisms confining RNA polymerase II ubiquitylation to polymerases undergoing transcriptional arrest. Cell 121, 913-923 (2005
    • (2005) Cell , vol.121 , pp. 913-923
    • Somesh, B.P.1
  • 113
    • 33947720525 scopus 로고    scopus 로고
    • Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD
    • Somesh, B.P. et al. Communication between distant sites in RNA polymerase II through ubiquitylation factors and the polymerase CTD. Cell 129, 57-68 (2007
    • (2007) Cell , vol.129 , pp. 57-68
    • Somesh, B.P.1
  • 114
    • 84883405887 scopus 로고    scopus 로고
    • Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress
    • Wilson, M.D. et al. Proteasome-mediated processing of Def1, a critical step in the cellular response to transcription stress. Cell 154, 983-995 (2013
    • (2013) Cell , vol.154 , pp. 983-995
    • Wilson, M.D.1
  • 115
    • 0037148786 scopus 로고    scopus 로고
    • A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage
    • Woudstra, E.C. et al. A Rad26-Def1 complex coordinates repair and RNA pol II proteolysis in response to DNA damage. Nature 415, 929-933 (2002
    • (2002) Nature , vol.415 , pp. 929-933
    • Woudstra, E.C.1
  • 116
    • 0034019810 scopus 로고    scopus 로고
    • Degradation of transcription factor IRF-1 by the ubiquitin-proteasome pathway: The C-Terminal region governs the protein stability
    • Nakagawa, K. & Yokosawa, H. Degradation of transcription factor IRF-1 by the ubiquitin-proteasome pathway: The C-Terminal region governs the protein stability. Eur. J. Biochem. 267, 1680-1686 (2000
    • (2000) Eur. J. Biochem , vol.267 , pp. 1680-1686
    • Nakagawa, K.1    Yokosawa, H.2
  • 117
  • 119
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland, U., Steinacher, R., Jiricny, J. & Schär, P. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21, 1456-1464 (2002
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schär, P.4
  • 120
    • 57749097697 scopus 로고    scopus 로고
    • Coordinating the initial steps of base excision repair: Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex
    • Fitzgerald, M.E. & Drohat, A.C. Coordinating the initial steps of base excision repair: Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex. J. Biol. Chem. 283, 32680-32690 (2008
    • (2008) J. Biol. Chem , vol.283 , pp. 32680-32690
    • Fitzgerald, M.E.1    Drohat, A.C.2
  • 121
    • 20544440797 scopus 로고    scopus 로고
    • Crystal structure of thymine DNA glycosylase conjugated to SUMO-1
    • Baba, D. et al. Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. Nature 435, 979-982 (2005
    • (2005) Nature , vol.435 , pp. 979-982
    • Baba, D.1
  • 122
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation
    • Steinacher, R. & Schar, P. Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr. Biol. 15, 616-623 (2005
    • (2005) Curr. Biol , vol.15 , pp. 616-623
    • Steinacher, R.1    Schar, P.2
  • 123
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites
    • Kapetanaki, M.G. et al. The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites. Proc. Natl. Acad. Sci. USA 103, 2588-2593 (2006
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1
  • 124
    • 33744781568 scopus 로고    scopus 로고
    • Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage
    • Wang, H. et al. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol. Cell 22, 383-394 (2006
    • (2006) Mol. Cell , vol.22 , pp. 383-394
    • Wang, H.1
  • 125
    • 84859485912 scopus 로고    scopus 로고
    • Monoubiquitinated histone H2A destabilizes photolesion-containing nucleosomes with concomitant release of UV-damaged DNA-binding protein E3 ligase
    • Lan, L. et al. Monoubiquitinated histone H2A destabilizes photolesion-containing nucleosomes with concomitant release of UV-damaged DNA-binding protein E3 ligase. J. Biol. Chem. 287, 12036-12049 (2012
    • (2012) J. Biol. Chem , vol.287 , pp. 12036-12049
    • Lan, L.1
  • 126
    • 33746324216 scopus 로고    scopus 로고
    • Chromatin modifications by methylation and ubiquitination: Implications in the regulation of gene expression
    • Shilatifard, A. Chromatin modifications by methylation and ubiquitination: Implications in the regulation of gene expression. Annu. Rev. Biochem. 75, 243-269 (2006
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 243-269
    • Shilatifard, A.1
  • 127
    • 84861558075 scopus 로고    scopus 로고
    • DNA robustly stimulates FANCD2 monoubiquitylation in the complex with FANCI
    • Sato, K., Toda, K., Ishiai, M., Takata, M. & Kurumizaka, H. DNA robustly stimulates FANCD2 monoubiquitylation in the complex with FANCI. Nucleic Acids Res. 40, 4553-4561 (2012.
    • (2012) Nucleic Acids Res , vol.40 , pp. 4553-4561
    • Sato, K.1    Toda, K.2    Ishiai, M.3    Takata, M.4    Kurumizaka, H.5


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