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Volumn 6, Issue , 2015, Pages

TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin

Author keywords

[No Author keywords available]

Indexed keywords

BRCA1 ASSOCIATED RING DOMAIN PROTEIN 1; DOUBLE STRANDED DNA; HISTONE H2AX; HISTONE H3; HISTONE H4; PROTEIN TRIM29; SCAFFOLD PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; BRAP PROTEIN, HUMAN; CHROMATIN; DMAP1 PROTEIN, HUMAN; DNA BINDING PROTEIN; DNA LIGASE; H2AFX PROTEIN, HUMAN; HISTONE; HISTONE ACETYLTRANSFERASE; HOMEODOMAIN PROTEIN; ING3 PROTEIN, HUMAN; KAT5 PROTEIN, HUMAN; MSH2 PROTEIN, HUMAN; NUCLEOSOME; PROTEIN MSH2; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TRIM29 PROTEIN, HUMAN; TUMOR SUPPRESSOR PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 84934963416     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8299     Document Type: Article
Times cited : (46)

References (49)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 78649446475 scopus 로고    scopus 로고
    • A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation
    • Dobbs, T. A., Tainer, J. A. & Lees-Miller, S. P. A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation. DNA Repair 9, 1307-1314 (2010).
    • (2010) DNA Repair , vol.9 , pp. 1307-1314
    • Dobbs, T.A.1    Tainer, J.A.2    Lees-Miller, S.P.3
  • 4
    • 78649445307 scopus 로고    scopus 로고
    • Mre11-Rad50-Nbs1 conformations and the control of sensing, signaling, and effector responses at DNA double-strand breaks
    • Williams, G. J., Lees-Miller, S. P. & Tainer, J. A. Mre11-Rad50-Nbs1 conformations and the control of sensing, signaling, and effector responses at DNA double-strand breaks. DNA Repair 9, 1299-1306 (2010).
    • (2010) DNA Repair , vol.9 , pp. 1299-1306
    • Williams, G.J.1    Lees-Miller, S.P.2    Tainer, J.A.3
  • 5
    • 65149084552 scopus 로고    scopus 로고
    • Crosstalk between histone modifications during the DNA damage response
    • van Attikum, H. & Gasser, S. M. Crosstalk between histone modifications during the DNA damage response. Trends Cell Biol. 19, 207-217 (2009).
    • (2009) Trends Cell Biol. , vol.19 , pp. 207-217
    • Van Attikum, H.1    Gasser, S.M.2
  • 6
    • 38049115657 scopus 로고    scopus 로고
    • The mechanism of human nonhomologous DNA end joining
    • Lieber, M. R. The mechanism of human nonhomologous DNA end joining. J. Biol. Chem. 283, 1-5 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 1-5
    • Lieber, M.R.1
  • 7
    • 50649100744 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo, J., Sung, P. & Klein, H. Mechanism of eukaryotic homologous recombination. Annu. Rev. Biochem. 77, 229-257 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 229-257
    • San Filippo, J.1    Sung, P.2    Klein, H.3
  • 8
    • 77957948991 scopus 로고    scopus 로고
    • DNA mismatch repair and the DNA damage response to ionizing radiation: Making sense of apparently conflicting data
    • Martin, L. M. et al. DNA mismatch repair and the DNA damage response to ionizing radiation: making sense of apparently conflicting data. Cancer Treat. Rev. 36, 518-527 (2010).
    • (2010) Cancer Treat. Rev. , vol.36 , pp. 518-527
    • Martin, L.M.1
  • 9
    • 0034655991 scopus 로고    scopus 로고
    • BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures
    • Wang, Y. et al. BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Genes Dev. 14, 927-939 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 927-939
    • Wang, Y.1
  • 10
    • 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
  • 11
    • 84878918708 scopus 로고    scopus 로고
    • The chromatin response to DNA breaks: Leaving a mark on genome integrity
    • Smeenk, G. & van Attikum, H. The chromatin response to DNA breaks: leaving a mark on genome integrity. Annu. Rev. Biochem. 82, 55-80 (2013).
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 55-80
    • Smeenk, G.1    Van Attikum, H.2
  • 12
    • 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).
    • (2013) Nature , vol.499 , pp. 50-54
    • Fradet-Turcotte, A.1
  • 13
    • 84875224166 scopus 로고    scopus 로고
    • Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination
    • Tang, J. et al. Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination. Nat. Struct. Mol. Biol. 20, 317-325 (2013).
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 317-325
    • Tang, J.1
  • 14
    • 79952256559 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining
    • Fnu, S. et al. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc. Natl Acad. Sci. USA 108, 540-545 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 540-545
    • Fnu, S.1
  • 15
    • 84897990643 scopus 로고    scopus 로고
    • Transcriptionally active chromatin recruits homologous recombination at DNA double-strand breaks
    • Aymard, F. et al. Transcriptionally active chromatin recruits homologous recombination at DNA double-strand breaks. Nat. Struct. Mol. Biol. 21, 366-374 (2014).
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 366-374
    • Aymard, F.1
  • 16
    • 84876943255 scopus 로고    scopus 로고
    • The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSalpha
    • Li, F. et al. The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSalpha. Cell 153, 590-600 (2013).
    • (2013) Cell , vol.153 , pp. 590-600
    • Li, F.1
  • 17
    • 84903451450 scopus 로고    scopus 로고
    • SETD2-dependent histone H3K36 trimethylation is required for homologous recombination repair and genome stability
    • Pfister, S. X. et al. SETD2-dependent histone H3K36 trimethylation is required for homologous recombination repair and genome stability. Cell Rep. 7, 2006-2018 (2014).
    • (2014) Cell Rep. , vol.7 , pp. 2006-2018
    • Pfister, S.X.1
  • 18
    • 0029057336 scopus 로고
    • A single ataxia telangiectasia gene with a product similar to PI-3 kinase
    • Savitsky, K. et al. A single ataxia telangiectasia gene with a product similar to PI-3 kinase. Science 268, 1749-1753 (1995).
    • (1995) Science , vol.268 , pp. 1749-1753
    • Savitsky, K.1
  • 19
    • 0026636702 scopus 로고
    • Cloning of a candidate gene for ataxia-telangiectasia group D
    • Kapp, L. N. et al. Cloning of a candidate gene for ataxia-telangiectasia group D. Am. J. Hum. Genet. 51, 45-54 (1992).
    • (1992) Am. J. Hum. Genet. , vol.51 , pp. 45-54
    • Kapp, L.N.1
  • 20
    • 80054848955 scopus 로고    scopus 로고
    • TRIM proteins and cancer
    • Hatakeyama, S. TRIM proteins and cancer. Nat. Rev. Cancer 11, 792-804 (2011).
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 792-804
    • Hatakeyama, S.1
  • 21
    • 77953416244 scopus 로고    scopus 로고
    • The ATDC (TRIM29) protein binds p53 and antagonizes p53-mediated functions
    • Yuan, Z. et al. The ATDC (TRIM29) protein binds p53 and antagonizes p53-mediated functions. Mol. Cell. Biol. 30, 3004-3015 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3004-3015
    • Yuan, Z.1
  • 22
    • 84896497591 scopus 로고    scopus 로고
    • ATDC/TRIM29 phosphorylation by ATM/MAPKAP kinase 2 mediates radioresistance in pancreatic cancer cells
    • Wang, L. et al. ATDC/TRIM29 phosphorylation by ATM/MAPKAP kinase 2 mediates radioresistance in pancreatic cancer cells. Cancer Res. 74, 1778-1788 (2014).
    • (2014) Cancer Res. , vol.74 , pp. 1778-1788
    • Wang, L.1
  • 23
    • 0029112667 scopus 로고
    • The product of the ataxia-telangiectasia group D complementing gene, ATDC, interacts with a protein kinase C substrate and inhibitor
    • Brzoska, P. M. et al. The product of the ataxia-telangiectasia group D complementing gene, ATDC, interacts with a protein kinase C substrate and inhibitor. Proc. Natl Acad. Sci. USA 92, 7824-7828 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7824-7828
    • Brzoska, P.M.1
  • 24
    • 79955658113 scopus 로고    scopus 로고
    • TRIM29 negatively regulates p53 via inhibition of Tip60
    • Sho, T. et al. TRIM29 negatively regulates p53 via inhibition of Tip60. Biochim. Biophys. Acta 1813, 1245-1253 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1245-1253
    • Sho, T.1
  • 25
    • 60649114313 scopus 로고    scopus 로고
    • Oncogenic function of ATDC in pancreatic cancer through Wnt pathway activation and beta-catenin stabilization
    • Wang, L. et al. Oncogenic function of ATDC in pancreatic cancer through Wnt pathway activation and beta-catenin stabilization. Cancer Cell 15, 207-219 (2009).
    • (2009) Cancer Cell , vol.15 , pp. 207-219
    • Wang, L.1
  • 26
    • 84904068372 scopus 로고    scopus 로고
    • TRIM29 as a novel prostate basal cell marker for diagnosis of prostate cancer
    • Kanno, Y. et al. TRIM29 as a novel prostate basal cell marker for diagnosis of prostate cancer. Acta Histochem. 116, 708-712 (2014).
    • (2014) Acta Histochem. , vol.116 , pp. 708-712
    • Kanno, Y.1
  • 27
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motif family identifies cell compartments
    • Reymond, A. et al. The tripartite motif family identifies cell compartments. EMBO J. 20, 2140-2151 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2140-2151
    • Reymond, A.1
  • 28
    • 47249100637 scopus 로고    scopus 로고
    • A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin
    • Aygun, O., Svejstrup, J. & Liu, Y. A RECQ5-RNA polymerase II association identified by targeted proteomic analysis of human chromatin. Proc. Natl Acad. Sci. USA 105, 8580-8584 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 8580-8584
    • Aygun, O.1    Svejstrup, J.2    Liu, Y.3
  • 29
    • 0037168586 scopus 로고    scopus 로고
    • Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
    • Strausberg, R. L. et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl Acad. Sci. USA 99, 16899-16903 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16899-16903
    • Strausberg, R.L.1
  • 30
    • 79959939884 scopus 로고    scopus 로고
    • Human mediator subunit MED26 functions as a docking site for transcription elongation factors
    • Takahashi, H. et al. Human mediator subunit MED26 functions as a docking site for transcription elongation factors. Cell 146, 92-104 (2011).
    • (2011) Cell , vol.146 , pp. 92-104
    • Takahashi, H.1
  • 31
    • 0037365789 scopus 로고    scopus 로고
    • ATM and related protein kinases: Safeguarding genome integrity
    • Shiloh, Y. ATM and related protein kinases: safeguarding genome integrity. Nat. Rev. Cancer 3, 155-168 (2003).
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 155-168
    • Shiloh, Y.1
  • 32
    • 77952563068 scopus 로고    scopus 로고
    • Condensin and cohesin complexity: The expanding repertoire of functions
    • Wood, A. J., Severson, A. F. & Meyer, B. J. Condensin and cohesin complexity: the expanding repertoire of functions. Nat. Rev. Genet. 11, 391-404 (2010).
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 391-404
    • Wood, A.J.1    Severson, A.F.2    Meyer, B.J.3
  • 33
    • 34248572591 scopus 로고    scopus 로고
    • Structure of the human MutSalpha DNA lesion recognition complex
    • Warren, J. J. et al. Structure of the human MutSalpha DNA lesion recognition complex. Mol. Cell 26, 579-592 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 579-592
    • Warren, J.J.1
  • 34
    • 38049125557 scopus 로고    scopus 로고
    • Mechanisms and functions of DNA mismatch repair
    • Li, G. M. Mechanisms and functions of DNA mismatch repair. Cell Res. 18, 85-98 (2008).
    • (2008) Cell Res. , vol.18 , pp. 85-98
    • Li, G.M.1
  • 35
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J. & Gay, N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951 (1982).
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 36
    • 0037412181 scopus 로고    scopus 로고
    • A conformational analysis of Walker motif A [GXXXXGKT (S)] in nucleotide-binding and other proteins
    • Ramakrishnan, C., Dani, V. S. & Ramasarma, T. A conformational analysis of Walker motif A [GXXXXGKT (S)] in nucleotide-binding and other proteins. Protein Eng. 15, 783-798 (2002).
    • (2002) Protein Eng. , vol.15 , pp. 783-798
    • Ramakrishnan, C.1    Dani, V.S.2    Ramasarma, T.3
  • 37
    • 0025048136 scopus 로고
    • The P-loop-A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P. R. & Wittinghofer, A. The P-loop-a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15, 430-434 (1990).
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 38
    • 84902168468 scopus 로고    scopus 로고
    • Regulating the chromatin landscape: Structural and mechanistic perspectives
    • Bartholomew, B. Regulating the chromatin landscape: structural and mechanistic perspectives. Annu. Rev. Biochem. 83, 671-696 (2014).
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 671-696
    • Bartholomew, B.1
  • 39
    • 0037226473 scopus 로고    scopus 로고
    • The mismatch repair system is required for S-phase checkpoint activation
    • Brown, K. D. et al. The mismatch repair system is required for S-phase checkpoint activation. Nat. Genet. 33, 80-84 (2003).
    • (2003) Nat. Genet. , vol.33 , pp. 80-84
    • Brown, K.D.1
  • 40
    • 0038297562 scopus 로고    scopus 로고
    • The mammalian mismatch repair protein MSH2 is required for correct MRE11 and RAD51 relocalization and for efficient cell cycle arrest induced by ionizing radiation in G2 phase
    • Franchitto, A. et al. The mammalian mismatch repair protein MSH2 is required for correct MRE11 and RAD51 relocalization and for efficient cell cycle arrest induced by ionizing radiation in G2 phase. Oncogene 22, 2110-2120 (2003).
    • (2003) Oncogene , vol.22 , pp. 2110-2120
    • Franchitto, A.1
  • 41
    • 84878944044 scopus 로고    scopus 로고
    • Readout of epigenetic modifications
    • Patel, D. J. & Wang, Z. Readout of epigenetic modifications. Annu. Rev. Biochem. 82, 81-118 (2013).
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 81-118
    • Patel, D.J.1    Wang, Z.2
  • 42
    • 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
  • 43
    • 23744447715 scopus 로고    scopus 로고
    • Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells
    • Kim, J. S. et al. Independent and sequential recruitment of NHEJ and HR factors to DNA damage sites in mammalian cells. J. Cell Biol. 170, 341-347 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 341-347
    • Kim, J.S.1
  • 44
    • 84863415403 scopus 로고    scopus 로고
    • Regulation of DNA-end resection by hnRNPU-like proteins promotes DNA double-strand break signaling and repair
    • Polo, S. E. et al. Regulation of DNA-end resection by hnRNPU-like proteins promotes DNA double-strand break signaling and repair. Mol. Cell 45, 505-516 (2012).
    • (2012) Mol. Cell , vol.45 , pp. 505-516
    • Polo, S.E.1
  • 45
    • 84886259963 scopus 로고    scopus 로고
    • The chromatin scaffold protein SAFB1 renders chromatin permissive for DNA damage signaling
    • Altmeyer, M. et al. The chromatin scaffold protein SAFB1 renders chromatin permissive for DNA damage signaling. Mol. Cell 52, 206-220 (2013).
    • (2013) Mol. Cell , vol.52 , pp. 206-220
    • Altmeyer, M.1
  • 46
    • 84860325854 scopus 로고    scopus 로고
    • Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response
    • Beli, P. et al. Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response. Mol. Cell 46, 212-225 (2012).
    • (2012) Mol. Cell , vol.46 , pp. 212-225
    • Beli, P.1
  • 47
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection
    • Albritton, L. M., Tseng, L., Scadden, D. & Cunningham, J. M. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection. Cell 57, 659-666 (1989).
    • (1989) Cell , vol.57 , pp. 659-666
    • Albritton, L.M.1    Tseng, L.2    Scadden, D.3    Cunningham, J.M.4
  • 48
    • 0034046944 scopus 로고    scopus 로고
    • Plat-E: An efficient and stable system for transient packaging of retroviruses
    • Morita, S., Kojima, T. & Kitamura, T. Plat-E: an efficient and stable system for transient packaging of retroviruses. Gene Ther. 7, 1063-1066 (2000).
    • (2000) Gene Ther. , vol.7 , pp. 1063-1066
    • Morita, S.1    Kojima, T.2    Kitamura, T.3
  • 49
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., Lebovitz, R. M. & Roeder, R. G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489 (1983).
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3


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