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Volumn 29, Issue 24, 2009, Pages 6335-6340

The emerging role of HP1 in the DNA damage response

Author keywords

[No Author keywords available]

Indexed keywords

HETEROCHROMATIN PROTEIN 1;

EID: 71949105212     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.01048-09     Document Type: Short Survey
Times cited : (95)

References (31)
  • 1
    • 33846493138 scopus 로고    scopus 로고
    • A structural rationale for stalling of a replicative DNA polymerase at the most common oxidative thymine lesion, thymine glycol
    • Aller, P., M. A. Rould, M. Hogg, S. S. Wallace, and S. Doublie. 2007. A structural rationale for stalling of a replicative DNA polymerase at the most common oxidative thymine lesion, thymine glycol. Proc. Natl. Acad. Sci. USA 104:814-818.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 814-818
    • Aller, P.1    Rould, M.A.2    Hogg, M.3    Wallace, S.S.4    Doublie, S.5
  • 3
    • 44449136965 scopus 로고    scopus 로고
    • HP1-beta mobilization promotes chromatin changes that initiate the DNA damage response
    • DOI 10.1038/nature06875, PII NATURE06875
    • Ayoub, N., A. D. Jeyasekharan, J. A. Bernal, and A. R. Venkitaraman. 2008. HP1-beta mobilization promotes chromatin changes that initiate the DNA damage response. Nature 453:682-686. (Pubitemid 351769293)
    • (2008) Nature , vol.453 , Issue.7195 , pp. 682-686
    • Ayoub, N.1    Jeyasekharan, A.D.2    Bernal, J.A.3    Venkitaraman, A.R.4
  • 4
    • 33847737716 scopus 로고    scopus 로고
    • DNA damage checkpoints: From initiation to recovery or adaptation
    • Bartek, J., and J. Lukas. 2007. DNA damage checkpoints: from initiation to recovery or adaptation. Curr. Opin. Cell Biol. 19:238-245.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 238-245
    • Bartek, J.1    Lukas, J.2
  • 5
    • 33644812489 scopus 로고    scopus 로고
    • Recognition of helical kinks by xeroderma pigmentosum group a protein triggers DNA excision repair
    • Camenisch, U., R. Dip, S. B. Schumacher, B. Schuler, and H. Naegeli. 2006. Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair. Nat. Struct. Mol. Biol. 13:278-284.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 278-284
    • Camenisch, U.1    Dip, R.2    Schumacher, S.B.3    Schuler, B.4    Naegeli, H.5
  • 6
    • 0348150714 scopus 로고    scopus 로고
    • Maintenance of stable heterochromatin domains by dynamic HP1 binding
    • DOI 10.1126/science.1078572
    • Cheutin, T., A. J. McNairn, T. Jenuwein, D. M. Gilbert, P. B. Singh, and T. Misteli. 2003. Maintenance of stable heterochromatin domains by dynamic HP1 binding. Science 299:721-725. (Pubitemid 36159490)
    • (2003) Science , vol.299 , Issue.5607 , pp. 721-725
    • Cheutin, T.1    McNairn, A.J.2    Jenuwein, T.3    Gilbert, D.M.4    Singh, P.B.5    Misteli, T.6
  • 7
    • 34247513888 scopus 로고    scopus 로고
    • Distinct Roles for the XPB/p52 and XPD/p44 Subcomplexes of TFIIH in Damaged DNA Opening during Nucleotide Excision Repair
    • DOI 10.1016/j.molcel.2007.03.009, PII S1097276507001542
    • Coin, F., V. Oksenych, and J. M. Egly. 2007. Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol. Cell 26:245-256. (Pubitemid 46656218)
    • (2007) Molecular Cell , vol.26 , Issue.2 , pp. 245-256
    • Coin, F.1    Oksenych, V.2    Egly, J.-M.3
  • 8
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • DOI 10.1093/emboj/16.21.6559
    • Evans, E., J. G. Moggs, J. R. Hwang, J. M. Egly, and R. D. Wood. 1997. Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J. 16:6559-6573. (Pubitemid 27483280)
    • (1997) EMBO Journal , vol.16 , Issue.21 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.-M.4    Wood, R.D.5
  • 9
    • 0038412822 scopus 로고    scopus 로고
    • The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase
    • DOI 10.1093/nar/gkg332
    • Fuks, F., P. J. Hurd, R. Deplus, and T. Kouzarides. 2003. The DNA methyltransferases associate with HP1 and the SUV39H1 histone methyltransferase. Nucleic Acids Res. 31:2305-2312. (Pubitemid 37442098)
    • (2003) Nucleic Acids Research , vol.31 , Issue.9 , pp. 2305-2312
    • Fuks, F.1    Hurd, P.J.2    Deplus, R.3    Kouzarides, T.4
  • 10
    • 47349107760 scopus 로고    scopus 로고
    • ATM signaling facilitates repair of DNA double-strand breaks associated with heterochromatin
    • Goodarzi, A. A., A. T. Noon, D. Deckbar, Y. Ziv, Y. Shiloh, M. Lobrich, and P. A. Jeggo. 2008. ATM signaling facilitates repair of DNA double-strand breaks associated with heterochromatin. Mol. Cell 31:167-177.
    • (2008) Mol. Cell , vol.31 , pp. 167-177
    • Goodarzi, A.A.1    Noon, A.T.2    Deckbar, D.3    Ziv, Y.4    Shiloh, Y.5    Lobrich, M.6    Jeggo, P.A.7
  • 11
  • 12
    • 39449092872 scopus 로고    scopus 로고
    • Quality control of DNA break metabolism: In the 'end', it's a good thing
    • Kanaar, R., C. Wyman, and R. Rothstein. 2008. Quality control of DNA break metabolism: in the 'end', it's a good thing. EMBO J. 27:581-588.
    • (2008) EMBO J. , vol.27 , pp. 581-588
    • Kanaar, R.1    Wyman, C.2    Rothstein, R.3
  • 13
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan, H. E., R. Standal, and G. Slupphaug. 1997. DNA glycosylases in the base excision repair of DNA. Biochem. J. 325:1-16. (Pubitemid 27322679)
    • (1997) Biochemical Journal , vol.325 , Issue.1 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 15
    • 1842733449 scopus 로고    scopus 로고
    • HP1 and the dynamics of heterochromatin maintenance
    • Maison, C., and G. Almouzni. 2004. HP1 and the dynamics of heterochromatin maintenance. Nat. Rev. Mol. Cell Biol. 5:296-304.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 296-304
    • Maison, C.1    Almouzni, G.2
  • 16
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison, C., D. Bailly, A. H. Peters, J. P. Quivy, D. Roche, A. Taddei, M. Lachner, T. Jenuwein, and G. Almouzni. 2002. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat. Genet. 30:329-334.
    • (2002) Nat. Genet. , vol.30 , pp. 329-334
    • Maison, C.1    Bailly, D.2    Peters, A.H.3    Quivy, J.P.4    Roche, D.5    Taddei, A.6    Lachner, M.7    Jenuwein, T.8    Almouzni, G.9
  • 17
    • 68249125947 scopus 로고    scopus 로고
    • 14-3-3 proteins, FHA domains and BRCT domains in the DNA damage response
    • Amsterdam
    • Mohammad, D. H., and M. B. Yaffe. 2009. 14-3-3 proteins, FHA domains and BRCT domains in the DNA damage response. DNA Repair (Amsterdam) 8:1009-1017.
    • (2009) DNA Repair , vol.8 , pp. 1009-1017
    • Mohammad, D.H.1    Yaffe, M.B.2
  • 18
    • 34447302016 scopus 로고    scopus 로고
    • Sealing of Chromosomal DNA Nicks during Nucleotide Excision Repair Requires XRCC1 and DNA Ligase IIIalpha in a Cell-Cycle-Specific Manner
    • DOI 10.1016/j.molcel.2007.06.014, PII S1097276507004042
    • Moser, J., H. Kool, I. Giakzidis, K. Caldecott, L. H. Mullenders, and M. I. Fousteri. 2007. Sealing of chromosomal DNA nicks during nucleotide excision repair requires XRCC1 and DNA ligase III alpha in a cell-cycle-specific manner. Mol. Cell 27:311-323. (Pubitemid 47058307)
    • (2007) Molecular Cell , vol.27 , Issue.2 , pp. 311-323
    • Moser, J.1    Kool, H.2    Giakzidis, I.3    Caldecott, K.4    Mullenders, L.H.F.5    Fousteri, M.I.6
  • 20
    • 0035019466 scopus 로고    scopus 로고
    • Heterochromatin formation in mammalian cells: Interaction between histones and HP1 Proteins
    • DOI 10.1016/S1097-2765(01)00218-0
    • Nielsen, A. L., M. Oulad-Abdelghani, J. A. Ortiz, E. Remboutsika, P. Chambon, and R. Losson. 2001. Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. Mol. Cell 7:729-739. (Pubitemid 32436434)
    • (2001) Molecular Cell , vol.7 , Issue.4 , pp. 729-739
    • Nielsen, A.L.1    Oulad-Abdelghani, M.2    Ortiz, J.A.3    Remboutsika, E.4    Chambon, P.5    Losson, R.6
  • 21
    • 51349099238 scopus 로고    scopus 로고
    • The HP1-p150/CAF-1 interaction is required for pericentric heterochromatin replication and S-phase progression in mouse cells
    • Quivy, J. P., A. Gerard, A. J. Cook, D. Roche, and G. Almouzni. 2008. The HP1-p150/CAF-1 interaction is required for pericentric heterochromatin replication and S-phase progression in mouse cells. Nat. Struct. Mol. Biol. 15:972-979.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 972-979
    • Quivy, J.P.1    Gerard, A.2    Cook, A.J.3    Roche, D.4    Almouzni, G.5
  • 22
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifications by linked binding modules
    • Ruthenburg, A. J., H. Li, D. J. Patel, and C. D. Allis. 2007. Multivalent engagement of chromatin modifications by linked binding modules. Nat. Rev. Mol. Cell Biol. 8:983-994.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    Allis, C.D.4
  • 24
    • 34249066239 scopus 로고    scopus 로고
    • Functional cooperation between HP1 and DNMT1 mediates gene silencing
    • DOI 10.1101/gad.1536807
    • Smallwood, A., P. O. Esteve, S. Pradhan, and M. Carey. 2007. Functional cooperation between HP1 and DNMT1 mediates gene silencing. Genes Dev. 21:1169-1178. (Pubitemid 46789875)
    • (2007) Genes and Development , vol.21 , Issue.10 , pp. 1169-1178
    • Smallwood, A.1    Esteve, P.-O.2    Pradhan, S.3    Carey, M.4
  • 25
    • 0037099413 scopus 로고    scopus 로고
    • G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
    • DOI 10.1101/gad.989402
    • Tachibana, M., K. Sugimoto, M. Nozaki, J. Ueda, T. Ohta, M. Ohki, M. Fukuda, N. Takeda, H. Niida, H. Kato, and Y. Shinkai. 2002. G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev. 16:1779-1791. (Pubitemid 34803894)
    • (2002) Genes and Development , vol.16 , Issue.14 , pp. 1779-1791
    • Tachibana, M.1    Sugimoto, K.2    Nozaki, M.3    Ueda, J.4    Ohta, T.5    Ohki, M.6    Fukuda, M.7    Takeda, N.8    Niida, H.9    Kato, H.10    Shinkai, Y.11
  • 29
    • 67649499996 scopus 로고    scopus 로고
    • Recruitment of heterochromatin protein 1 to DNA repair sites
    • Zarebski, M., E. Wiernasz, and J. W. Dobrucki. 2009. Recruitment of heterochromatin protein 1 to DNA repair sites. Cytometry A 75:619-625.
    • (2009) Cytometry A , vol.75 , pp. 619-625
    • Zarebski, M.1    Wiernasz, E.2    Dobrucki, J.W.3
  • 30
    • 33846604273 scopus 로고    scopus 로고
    • HP1 proteins are essential for a dynamic nuclear response that rescues the function of perturbed heterochromatin in primary human cells
    • Zhang, R., S. T. Liu, W. Chen, M. Bonner, J. Pehrson, T. J. Yen, and P. D. Adams. 2007. HP1 proteins are essential for a dynamic nuclear response that rescues the function of perturbed heterochromatin in primary human cells. Mol. Cell. Biol. 27:949-962.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 949-962
    • Zhang, R.1    Liu, S.T.2    Chen, W.3    Bonner, M.4    Pehrson, J.5    Yen, T.J.6    Adams, P.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.