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Volumn 3, Issue OCT, 2013, Pages

SET7/9-dependent methylation of ARTD1 at K508 stimulates poly-ADP-ribose formation after oxidative stress

Author keywords

ADP ribosylation; Lysine methylation; PARP 1; Protein regulation; SET7 9

Indexed keywords

HISTONE; HISTONE LYSINE METHYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP1 PROTEIN, HUMAN; POLY(ADENOSINE DIPHOSPHATE RIBOSE);

EID: 84885636888     PISSN: None     EISSN: 20462441     Source Type: Journal    
DOI: 10.1098/rsob.120173     Document Type: Article
Times cited : (40)

References (44)
  • 1
    • 77951023118 scopus 로고    scopus 로고
    • Toward a unified nomenclature for mammalian ADP-ribosyltransferases
    • doi:10.1016/j.tibs.2009.12.003
    • Hottiger MO, Hassa PO, Lüscher B, Schüler H, Koch-Nolte F. 2010 Toward a unified nomenclature for mammalian ADP-ribosyltransferases. Trends Biochem. Sci. 35, 208-219. (doi:10.1016/j.tibs.2009.12.003)
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 208-219
    • Hottiger, M.O.1    Hassa, P.O.2    Lüscher, B.3    Schüler, H.4    Koch-Nolte, F.5
  • 2
    • 70350548179 scopus 로고    scopus 로고
    • Sumoylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function
    • doi:10.1096/fj.09-137695
    • Messner S, Schuermann D, Altmeyer M, Kassner I, Schmidt D, Schär P, Müller S, Hottiger MO. 2009 Sumoylation of poly(ADP-ribose) polymerase 1 inhibits its acetylation and restrains transcriptional coactivator function. FASEB J. 23, 3978-3989. (doi:10.1096/fj.09-137695)
    • (2009) FASEB J. , vol.23 , pp. 3978-3989
    • Messner, S.1    Schuermann, D.2    Altmeyer, M.3    Kassner, I.4    Schmidt, D.5    Schär, P.6    Müller, S.7    Hottiger, M.O.8
  • 3
    • 28844493947 scopus 로고    scopus 로고
    • Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-κB-dependent transcription
    • DOI 10.1074/jbc.M507553200
    • Hassa PO, Haenni SS, Buerki C, Meier NI, Lane WS, Owen H, Gersbach M, Imhof R, Hottiger MO. 2005 Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-κB-dependent transcription. J. Biol. Chem. 280, 40 450-40 464. (doi:10.1074/jbc.M507553200) (Pubitemid 41780532)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40450-40464
    • Hassa, P.O.1    Haenni, S.S.2    Buerki, C.3    Meier, N.I.4    Lane, W.S.5    Owen, H.6    Gersbach, M.7    Imhof, R.8    Hottiger, M.O.9
  • 4
    • 67649888368 scopus 로고    scopus 로고
    • Molecular mechanism of poly(ADPribosyl) ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites
    • doi:10.1093/nar/gkp229
    • Altmeyer M, Messner S, Hassa PO, Fey M, Hottiger MO. 2009 Molecular mechanism of poly(ADPribosyl) ation by PARP1 and identification of lysine residues as ADP-ribose acceptor sites. Nucleic Acids Res. 37, 3723-3738. (doi:10.1093/nar/gkp229)
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3723-3738
    • Altmeyer, M.1    Messner, S.2    Hassa, P.O.3    Fey, M.4    Hottiger, M.O.5
  • 5
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: Where are we today and where are we going?
    • DOI 10.1128/MMBR.00040-05
    • Hassa PO, Haenni S, Elser M, Hottiger MO. 2006 Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? Microbiol. Mol. Biol. Rev. 70, 789-829. (doi:10.1128/MMBR.00040-05) (Pubitemid 44484693)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.3 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 6
    • 77956648852 scopus 로고    scopus 로고
    • The roles of PARP1 in gene control and cell differentiation
    • doi:10.1016/j.gde.2010.06.001
    • Ji Y, Tulin A. 2010 The roles of PARP1 in gene control and cell differentiation. Curr. Opin. Genet. Dev. 20, 512-518. (doi:10.1016/j.gde.2010. 06.001)
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 512-518
    • Ji, Y.1    Tulin, A.2
  • 8
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • DOI 10.1042/0264-6021:3420249
    • D'Amours D, Desnoyers S, D'Silva I, Poirier G. 1999 Poly(ADP-ribosyl) ation reactions in the regulation of nuclear functions. Biochem. J. 342, 249-268. (doi:10.1042/0264-6021:3420249) (Pubitemid 29425344)
    • (1999) Biochemical Journal , vol.342 , Issue.2 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 9
    • 0018786089 scopus 로고
    • Poly(ADP-ribosy)ation of nuclear proteins. Enzymatic elongation of chemically synthesized ADP-ribosehistone adducts
    • Ueda K, Kawaichi M, Okayama H, Hayaishi O. 1979 Poly(ADP-ribosy)ation of nuclear proteins. Enzymatic elongation of chemically synthesized ADP-ribosehistone adducts. J. Biol. Chem. 254, 679-687.
    • (1979) J. Biol. Chem. , vol.254 , pp. 679-687
    • Ueda, K.1    Kawaichi, M.2    Okayama, H.3    Hayaishi, O.4
  • 10
    • 84857891632 scopus 로고    scopus 로고
    • On PAR with PARP: Cellular stress signaling through poly(ADP-ribose) and PARP-1
    • doi:10.1101/gad.183509.111
    • Luo X, Kraus WL. 2012 On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1. Genes Dev. 26, 417-432. (doi:10.1101/gad.183509. 111)
    • (2012) Genes Dev. , vol.26 , pp. 417-432
    • Luo, X.1    Kraus, W.L.2
  • 11
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • DOI 10.1016/S1097-2765(01)00405-1
    • Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y. 2001 Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell 8, 1207-1217. (doi:10.1016/S1097- 2765(01)00405-1) (Pubitemid 34084993)
    • (2001) Molecular Cell , vol.8 , Issue.6 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 12
    • 65549170303 scopus 로고    scopus 로고
    • Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with geneactivating epigenetic marks that coexist on the lysine tail
    • doi:10.2337/db08-1666
    • Brasacchio D et al. 2009 Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with geneactivating epigenetic marks that coexist on the lysine tail. Diabetes 58, 1229-1236. (doi:10.2337/db08-1666)
    • (2009) Diabetes , vol.58 , pp. 1229-1236
    • Brasacchio, D.1
  • 13
    • 63249112026 scopus 로고    scopus 로고
    • Methyltransferase Set7/9 maintains transcription and euchromatin structure at isletenriched genes
    • doi:10.2337/db08-1150
    • Deering TG, Ogihara T, Trace AP, Maier B, Mirmira RG. 2009 Methyltransferase Set7/9 maintains transcription and euchromatin structure at isletenriched genes. Diabetes 58, 185-193. (doi:10.2337/db08-1150)
    • (2009) Diabetes , vol.58 , pp. 185-193
    • Deering, T.G.1    Ogihara, T.2    Trace, A.P.3    Maier, B.4    Mirmira, R.G.5
  • 14
    • 55549140173 scopus 로고    scopus 로고
    • Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation
    • doi:10.1074/jbc.M802800200
    • Li Y, Reddy MA, Miao F, Shanmugam N, Yee JK, Hawkins D, Ren B, Natarajan R. 2008 Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation. J. Biol. Chem. 283, 26 771-26 781. (doi:10.1074/jbc.M802800200)
    • (2008) J. Biol. Chem. , vol.283 , pp. 26771-26781
    • Li, Y.1    Reddy, M.A.2    Miao, F.3    Shanmugam, N.4    Yee, J.K.5    Hawkins, D.6    Ren, B.7    Natarajan, R.8
  • 17
    • 38949178369 scopus 로고    scopus 로고
    • Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo
    • DOI 10.1016/j.molcel.2007.12.025, PII S1097276508000683
    • Kurash J, Lei H, Shen Q, Marston W, Granda B, Fan H, Wall D, Li E, Gaudet F. 2008 Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo. Mol. Cell 29, 392-400. (doi:10.1016/j.molcel.2007.12.025) (Pubitemid 351215939)
    • (2008) Molecular Cell , vol.29 , Issue.3 , pp. 392-400
    • Kurash, J.K.1    Lei, H.2    Shen, Q.3    Marston, W.L.4    Granda, B.W.5    Fan, H.6    Wall, D.7    Li, E.8    Gaudet, F.9
  • 18
    • 32244444118 scopus 로고    scopus 로고
    • Structural basis for the methylation site specificity of SET7/9
    • DOI 10.1038/nsmb1045, PII NSMB1045
    • Couture JF, Collazo E, Hauk G, Trievel RC. 2006 Structural basis for the methylation site specificity of SET7/9. Nat. Struct. Mol. Biol. 13, 140-146. (doi:10.1038/nsmb1045) (Pubitemid 43214717)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.2 , pp. 140-146
    • Couture, J.-F.1    Collazo, E.2    Hauk, G.3    Trievel, R.C.4
  • 19
    • 73149099403 scopus 로고    scopus 로고
    • Regulation of NF-κB activity through lysine monomethylation of p65
    • doi:10.1073/pnas.0910439106
    • Ea C, Baltimore D. 2009 Regulation of NF-κB activity through lysine monomethylation of p65. Proc. Natl Acad. Sci. USA 105, 18 972-18 977. (doi:10.1073/pnas.0910439106)
    • (2009) Proc. Natl Acad. Sci. USA , vol.105 , pp. 18972-18977
    • Ea, C.1    Baltimore, D.2
  • 20
    • 77951623834 scopus 로고    scopus 로고
    • Lysine methylation regulates the pRb tumour suppressor protein
    • doi:10.1038/onc.2009.511
    • Munro S, Khaire N, Inche A, Carr S, La Thangue N. 2010 Lysine methylation regulates the pRb tumour suppressor protein. Oncogene 29, 2357-2367. (doi:10.1038/onc.2009.511)
    • (2010) Oncogene , vol.29 , pp. 2357-2367
    • Munro, S.1    Khaire, N.2    Inche, A.3    Carr, S.4    La Thangue, N.5
  • 21
    • 77749342901 scopus 로고    scopus 로고
    • The Cellular lysine methyltransferase Set7/9-KMT7 binds HIV-1 TAR RNA, monomethylates the viral transactivator Tat, and enhances HIV transcription
    • doi:10.1016/j.chom.2010.02.005
    • Pagans S et al. 2010 The Cellular lysine methyltransferase Set7/9-KMT7 binds HIV-1 TAR RNA, monomethylates the viral transactivator Tat, and enhances HIV transcription. Cell Host Microbe 7, 234-244. (doi:10.1016/j.chom.2010.02. 005)
    • (2010) Cell Host Microbe , vol.7 , pp. 234-244
    • Pagans, S.1
  • 22
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • DOI 10.1016/S1097-2765(04)00182-0, PII S1097276504001820
    • Kouskouti A, Scheer E, Staub A, Tora L, Talianidis I. 2004 Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol. Cell 14, 175-182. (doi:10.1016/S1097-2765(04)00182-0) (Pubitemid 38515645)
    • (2004) Molecular Cell , vol.14 , Issue.2 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 24
    • 80052635380 scopus 로고    scopus 로고
    • The histone methyltransferase Set7/9 promotes myoblast differentiation and myofibril assembly
    • doi:10.1083/jcb.201010090
    • Tao Y, Neppl RL, Huang ZP, Chen J, Tang RH, Cao R, Zhang Y, Jin SW, Wang DZ. 2011 The histone methyltransferase Set7/9 promotes myoblast differentiation and myofibril assembly. J. Cell Biol. 194, 551-565. (doi:10.1083/jcb.201010090)
    • (2011) J. Cell Biol. , vol.194 , pp. 551-565
    • Tao, Y.1    Neppl, R.L.2    Huang, Z.P.3    Chen, J.4    Tang, R.H.5    Cao, R.6    Zhang, Y.7    Jin, S.W.8    Wang, D.Z.9
  • 25
    • 79251590753 scopus 로고    scopus 로고
    • Specificity analysis-based identification of new methylation targets of the SET7/9 protein lysine methyltransferase
    • doi:10.1016/j.chembiol.2010.11.014
    • Dhayalan A, Kudithipudi S, Rathert P, Jeltsch A. 2011 Specificity analysis-based identification of new methylation targets of the SET7/9 protein lysine methyltransferase. Chem. Biol. 18, 111-120. (doi:10.1016/j.chembiol.2010. 11.014)
    • (2011) Chem. Biol. , vol.18 , pp. 111-120
    • Dhayalan, A.1    Kudithipudi, S.2    Rathert, P.3    Jeltsch, A.4
  • 26
    • 80051733367 scopus 로고    scopus 로고
    • P53-dependent transcription and tumor suppression are not affected in Set7/9-deficient mice
    • doi:10.1016/j.molcel.2011.08.006
    • Lehnertz B, Rogalski JC, Schulze FM, Yi L, Lin S, Kast J, Rossi FM. 2011 p53-dependent transcription and tumor suppression are not affected in Set7/9-deficient mice. Mol. Cell 43, 673-680. (doi:10.1016/j.molcel.2011.08.006)
    • (2011) Mol. Cell , vol.43 , pp. 673-680
    • Lehnertz, B.1    Rogalski, J.C.2    Schulze, F.M.3    Yi, L.4    Lin, S.5    Kast, J.6    Rossi, F.M.7
  • 27
    • 80051733486 scopus 로고    scopus 로고
    • The methyltransferase Set7/9 (Setd7) is dispensable for the p53-mediated DNA damage response in vivo
    • doi:10.1016/j.molcel.2011.08.007
    • Campaner S, Spreafico F, Burgold T, Doni M, Rosato U, Amati B, Testa G. 2011 The methyltransferase Set7/9 (Setd7) is dispensable for the p53-mediated DNA damage response in vivo. Mol. Cell 43, 681-688. (doi:10.1016/j.molcel.2011. 08.007)
    • (2011) Mol. Cell , vol.43 , pp. 681-688
    • Campaner, S.1    Spreafico, F.2    Burgold, T.3    Doni, M.4    Rosato, U.5    Amati, B.6    Testa, G.7
  • 29
    • 58149156264 scopus 로고    scopus 로고
    • The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation
    • doi:10.1038/ng.268
    • Wang J et al. 2009 The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation. Nat. Genet. 41, 125-129. (doi:10.1038/ng.268)
    • (2009) Nat. Genet. , vol.41 , pp. 125-129
    • Wang, J.1
  • 31
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, Casero RA. 2004 Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941-953. (doi:10.1016/j.cell.2004.12.012) (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 32
    • 77956153243 scopus 로고    scopus 로고
    • The language of histone crosstalk
    • doi:10.1016/j.cell.2010.08.011
    • Lee JS, Smith E, Shilatifard A. 2010 The language of histone crosstalk. Cell 142, 682-685. (doi:10.1016/j.cell.2010.08.011)
    • (2010) Cell , vol.142 , pp. 682-685
    • Lee, J.S.1    Smith, E.2    Shilatifard, A.3
  • 33
    • 65149084552 scopus 로고    scopus 로고
    • Crosstalk between histone modifications during the DNA damage response
    • doi:10.1016/j.tcb.2009.03.001
    • van Attikum H, Gasser SM. 2009 Crosstalk between histone modifications during the DNA damage response. Trends Cell Biol. 19, 207-217. (doi:10.1016/j.tcb.2009.03.001)
    • (2009) Trends Cell Biol. , vol.19 , pp. 207-217
    • Van Attikum, H.1    Gasser, S.M.2
  • 34
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: Codified crosstalk with other posttranslational modifications
    • doi:10.1016/j.molcel.2008.07.002
    • Yang X-J, Seto E. 2008 Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 31, 449-461. (doi:10.1016/j.molcel. 2008.07.002)
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.-J.1    Seto, E.2
  • 35
    • 77951213317 scopus 로고    scopus 로고
    • Specific local induction of DNA strand breaks by infrared multi-photon absorption
    • doi:10.1093/nar/gkp932
    • Trautlein D, Deibler M, Leitenstorfer A, Ferrando-May E. 2010 Specific local induction of DNA strand breaks by infrared multi-photon absorption. Nucleic Acids Res. 38, e14. (doi:10.1093/nar/gkp932)
    • (2010) Nucleic Acids Res. , vol.38
    • Trautlein, D.1    Deibler, M.2    Leitenstorfer, A.3    Ferrando-May, E.4
  • 36
    • 69949133036 scopus 로고    scopus 로고
    • A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation
    • doi:10.1038/nsmb.1664
    • Timinszky G et al. 2009 A macrodomain-containing histone rearranges chromatin upon sensing PARP1 activation. Nat. Struct. Mol. Biol. 16, 923-929. (doi:10.1038/nsmb.1664)
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 923-929
    • Timinszky, G.1
  • 37
    • 77956526559 scopus 로고    scopus 로고
    • PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway
    • doi:10.1016/j.molcel.2010.08.014
    • Krishnakumar R, Kraus W. 2010 PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway. Mol. Cell 39, 736-749. (doi:10.1016/j.molcel.2010.08.014)
    • (2010) Mol. Cell , vol.39 , pp. 736-749
    • Krishnakumar, R.1    Kraus, W.2
  • 38
    • 0242496900 scopus 로고    scopus 로고
    • Transcriptional coactivation of nuclear factor-κB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1
    • DOI 10.1074/jbc.M307957200
    • Hassa PO, Buerki C, Lombardi C, Imhof R, Hottiger MO. 2003 Transcriptional coactivation of nuclear factorκB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1. J. Biol. Chem. 278, 45 145-45 153. (doi:10.1074/jbc.M307957200) (Pubitemid 37432647)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45145-45153
    • Hassa, P.O.1    Buerki, C.2    Lombardi, C.3    Imhof, R.4    Hottiger, M.O.5
  • 39
    • 33645979651 scopus 로고    scopus 로고
    • Arginine methylation regulates DNA polymerase b
    • doi:10.1016/j.molcel.2006.02.013
    • El-Andaloussi N et al. 2006 Arginine methylation regulates DNA polymerase b. Mol. Cell 22, 51-62. (doi:10.1016/j.molcel.2006.02.013)
    • (2006) Mol. Cell , vol.22 , pp. 51-62
    • El-Andaloussi, N.1
  • 40
    • 0029074364 scopus 로고
    • BM28, a human member of the MCM2-3-5 family, is displaced from chromatin during DNA replication
    • doi:10.1083/jcb.129.6.1433
    • Todorov IT, Attaran A, Kearsey SE. 1995 BM28, a human member of the MCM2-3-5 family, is displaced from chromatin during DNA replication. J. Cell Biol. 129, 1433-1445. (doi:10.1083/jcb.129.6.1433)
    • (1995) J. Cell Biol. , vol.129 , pp. 1433-1445
    • Todorov, I.T.1    Attaran, A.2    Kearsey, S.E.3
  • 42
    • 0027934998 scopus 로고
    • Transcription factor AP-2 regulates human immunodeficiency virus type 1 gene expression
    • Perkins ND, Agranoff AB, Duckett CS, Nabel GJ. 1994 Transcription factor AP-2 regulates human immunodeficiency virus type 1 gene expression. J. Virol. 68, 6820-6823. (Pubitemid 24294941)
    • (1994) Journal of Virology , vol.68 , Issue.10 , pp. 6820-6823
    • Perkins, N.D.1    Agranoff, A.B.2    Duckett, C.S.3    Nabel, G.J.4


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