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Volumn 13, Issue 22, 2014, Pages 3551-3564

Dynamics of re-constitution of the human nuclear proteome after cell division is regulated by NLS-adjacent phosphorylation

Author keywords

Cell cycle; DUTPase; Importin; Phosphorylation; Trafficking

Indexed keywords

CYCLIN DEPENDENT KINASE 1; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DNA; PROTEOME; RNA; CDK1 PROTEIN, HUMAN; CYCLIN DEPENDENT KINASE; NUCLEAR LOCALIZATION SIGNAL;

EID: 84919904530     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/15384101.2014.960740     Document Type: Article
Times cited : (22)

References (86)
  • 1
    • 0029059548 scopus 로고
    • Distinct functions for the two importin subunits in nuclear protein import
    • PMID:7675110
    • Gorlich D, Vogel F, Mills AD, Hartmann E, Laskey RA. Distinct functions for the two importin subunits in nuclear protein import. Nature 1995; 377:246-8; PMID:7675110; http://dx.doi.org/10.1038/377246a0
    • (1995) Nature , vol.377 , pp. 246-248
    • Gorlich, D.1    Vogel, F.2    Mills, A.D.3    Hartmann, E.4    Laskey, R.A.5
  • 2
    • 38349187678 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport of proteins
    • PMID:18282135
    • Sorokin AV, Kim ER, Ovchinnikov LP. Nucleocytoplasmic transport of proteins. Biochem Biokhimiia 2007; 72:1439-57; PMID:18282135; http://dx.doi. org/10.1134/S0006297907130032
    • (2007) Biochem Biokhimiia , vol.72 , pp. 1439-1457
    • Sorokin, A.V.1    Kim, E.R.2    Ovchinnikov, L.P.3
  • 3
    • 0028802362 scopus 로고
    • The regulation of protein transport to the nucleus by phosphorylation
    • PMID:7487922
    • Jans DA. The regulation of protein transport to the nucleus by phosphorylation. Biochem J 1995; 311 (Pt 3):705-16; PMID:7487922
    • (1995) Biochem J , vol.311 , Issue.3 , pp. 705-716
    • Jans, D.A.1
  • 4
    • 0029797971 scopus 로고    scopus 로고
    • Regulation of protein transport to the nucleus: Central role of phosphorylation
    • PMID:8757785
    • Jans DA, Hubner S. Regulation of protein transport to the nucleus: central role of phosphorylation. Physiol Rev 1996; 76:651-85; PMID:8757785
    • (1996) Physiol Rev , vol.76 , pp. 651-685
    • Jans, D.A.1    Hubner, S.2
  • 5
    • 78650333751 scopus 로고    scopus 로고
    • Phosphorylation meets nuclear import: A review
    • PMID:21182795
    • Nardozzi JD, Lott K, Cingolani G. Phosphorylation meets nuclear import: a review. Cell Commun Signal: CCS 2010; 8:32; PMID:21182795; http://dx.doi.org/ 10.1186/1478-811X-8-32
    • (2010) Cell Commun Signal: CCS , vol.8 , pp. 32
    • Nardozzi, J.D.1    Lott, K.2    Cingolani, G.3
  • 6
    • 67649845784 scopus 로고    scopus 로고
    • Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs
    • PMID:19520826
    • Kosugi S, Hasebe M, Tomita M, Yanagawa H. Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc Nat Acad Sci U S A 2009; 106:10171-6; PMID:19520826; http://dx.doi.org/ 10.1073/pnas.0900604106
    • (2009) Proc Nat Acad Sci U S A , vol.106 , pp. 10171-10176
    • Kosugi, S.1    Hasebe, M.2    Tomita, M.3    Yanagawa, H.4
  • 7
    • 0041845285 scopus 로고    scopus 로고
    • Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha
    • PMID:12695505
    • Fontes MR, Teh T, Jans D, Brinkworth RI, Kobe B. Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha. J Biol Chem 2003; 278:27981-7; PMID:12695505; http:// dx.doi.org/10.1074/jbc.M303275200
    • (2003) J Biol Chem , vol.278 , pp. 27981-27987
    • Fontes, M.R.1    Teh, T.2    Jans, D.3    Brinkworth, R.I.4    Kobe, B.5
  • 8
    • 29144510554 scopus 로고    scopus 로고
    • Substrate specificity of protein kinases and computational prediction of substrates
    • PMID:16172032
    • Kobe B, Kampmann T, Forwood JK, Listwan P, Brinkworth RI. Substrate specificity of protein kinases and computational prediction of substrates. Biochim Biophys Acta 2005; 1754:200-9; PMID:16172032; http://dx.doi.org/10.1016/j.bbapap.2005.07.036
    • (2005) Biochim Biophys Acta , vol.1754 , pp. 200-209
    • Kobe, B.1    Kampmann, T.2    Forwood, J.K.3    Listwan, P.4    Brinkworth, R.I.5
  • 9
    • 15444372337 scopus 로고    scopus 로고
    • Protein kinase specificity. A strategic collaboration between kinase peptide specificity and substrate recruitment
    • PMID:15655379
    • Zhu G, Liu Y, Shaw S. Protein kinase specificity. A strategic collaboration between kinase peptide specificity and substrate recruitment. Cell Cycle 2005; 4:52-6; PMID:15655379; http://dx.doi.org/10.4161/cc.4.1.1353
    • (2005) Cell Cycle , vol.4 , pp. 52-56
    • Zhu, G.1    Liu, Y.2    Shaw, S.3
  • 10
    • 0029819179 scopus 로고    scopus 로고
    • A predictive scale for evaluating cyclin-dependent kinase substrates. A comparison of p34cdc2 and p33cdk2
    • PMID:8810285
    • Holmes JK, Solomon MJ. A predictive scale for evaluating cyclin-dependent kinase substrates. A comparison of p34cdc2 and p33cdk2. J Biol Chem 1996; 271:25240-6; PMID:8810285; http://dx.doi. org/10.1074/jbc.271.41.25240
    • (1996) J Biol Chem , vol.271 , pp. 25240-25246
    • Holmes, J.K.1    Solomon, M.J.2
  • 11
    • 0027186606 scopus 로고
    • Cellular substrates of p34(cdc2) and its companion cyclin-dependent kinases
    • PMID:14731846
    • Nigg EA. Cellular substrates of p34(cdc2) and its companion cyclin-dependent kinases. Trends Cell Biol 1993; 3:296-301; PMID:14731846; http://dx.doi.org/ 10.1016/0962-8924(93)90011-O
    • (1993) Trends Cell Biol , vol.3 , pp. 296-301
    • Nigg, E.A.1
  • 12
    • 0028540405 scopus 로고
    • Use of an oriented peptide library to determine the optimal substrates of protein kinases
    • PMID:7874496
    • Songyang Z, Blechner S, Hoagland N, Hoekstra MF, Piwnica-Worms H, Cantley LC. Use of an oriented peptide library to determine the optimal substrates of protein kinases. Curr Biol: CB 1994; 4:973-82; PMID:7874496; http://dx.doi.org/10.1016/S0960-9822(00)00221-9
    • (1994) Curr Biol: CB , vol.4 , pp. 973-982
    • Songyang, Z.1    Blechner, S.2    Hoagland, N.3    Hoekstra, M.F.4    Piwnica-Worms, H.5    Cantley, L.C.6
  • 13
    • 79960876979 scopus 로고    scopus 로고
    • Predicting protein kinase specificity: Predikin update and performance in the DREAM4 challenge
    • PMID: 21829434
    • Ellis JJ, Kobe B. Predicting protein kinase specificity: Predikin update and performance in the DREAM4 challenge. PLoS One 2011; 6:e21169; PMID: 21829434; http://dx.doi.org/10.1371/journal.pone. 0021169
    • (2011) PLoS One , vol.6 , pp. e21169
    • Ellis, J.J.1    Kobe, B.2
  • 14
    • 0037422596 scopus 로고    scopus 로고
    • Structural basis and prediction of substrate specificity in protein serine/threonine kinases
    • PMID:12502784
    • Brinkworth RI, Breinl RA, Kobe B. Structural basis and prediction of substrate specificity in protein serine/threonine kinases. Proc Natl Acad Sci U S A 2003; 100:74-9; PMID:12502784; http://dx.doi.org/10.1073/pnas. 0134224100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 74-79
    • Brinkworth, R.I.1    Breinl, R.A.2    Kobe, B.3
  • 15
    • 84866925795 scopus 로고    scopus 로고
    • Computational modelling of linear motif-mediated protein interactions
    • PMID:22827524
    • Kobe B, Boden M. Computational modelling of linear motif-mediated protein interactions. Curr Topics Med Chem 2012; 12:1553-61; PMID:22827524; http://dx. doi.org/10.2174/156802612802652439
    • (2012) Curr Topics Med Chem , vol.12 , pp. 1553-1561
    • Kobe, B.1    Boden, M.2
  • 16
    • 79954464545 scopus 로고    scopus 로고
    • A probabilistic model of nuclear import of proteins
    • PMID:21372083
    • Mehdi AM, Sehgal MS, Kobe B, Bailey TL, Boden M. A probabilistic model of nuclear import of proteins. Bioinformatics 2011; 27:1239-46; PMID:21372083; http://dx.doi.org/10.1093/bioinformatics/btr121
    • (2011) Bioinformatics , vol.27 , pp. 1239-1246
    • Mehdi, A.M.1    Sehgal, M.S.2    Kobe, B.3    Bailey, T.L.4    Boden, M.5
  • 17
    • 44849086809 scopus 로고    scopus 로고
    • Predikin and PredikinDB: A computational framework for the prediction of protein kinase peptide specificity and an associated database of phosphorylation sites
    • PMID:18501020
    • Saunders NF, Brinkworth RI, Huber T, Kemp BE, Kobe B. Predikin and PredikinDB: A computational framework for the prediction of protein kinase peptide specificity and an associated database of phosphorylation sites. BMC Bioinformatics 2008; 9:245; PMID:18501020; http://dx.doi.org/10.1186/1471-2105-9-245
    • (2008) BMC Bioinformatics , vol.9 , pp. 245
    • Saunders, N.F.1    Brinkworth, R.I.2    Huber, T.3    Kemp, B.E.4    Kobe, B.5
  • 18
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based profile scanning approach for genome-wide prediction of signaling pathways
    • Yaffe MB, Leparc GG, Lai J, Obata T, Volinia S, Cantley LC. A motif-based profile scanning approach for genome-wide prediction of signaling pathways. Nat Biotechnol 2001; 19:348-53.; http://dx.doi.org/10. 1038/86737
    • (2001) Nat Biotechnol , vol.19 , pp. 348-353
    • Yaffe, M.B.1    Leparc, G.G.2    Lai, J.3    Obata, T.4    Volinia, S.5    Cantley, L.C.6
  • 19
    • 0030883687 scopus 로고    scopus 로고
    • The spindle pole body of Schizosaccharomyces pombe enters and leaves the nuclear envelope as the cell cycle proceeds
    • PMID:9285819
    • Ding R, West RR,Morphew DM, Oakley BR, McIntosh JR. The spindle pole body of Schizosaccharomyces pombe enters and leaves the nuclear envelope as the cell cycle proceeds. Mol Biol Cell 1997; 8:1461-79; PMID:9285819; http://dx.doi.org/10.1091/mbc.8.8.1461
    • (1997) Mol Biol Cell , vol.8 , pp. 1461-1479
    • Ding, R.1    West, R.R.2    Morphew, D.M.3    Oakley, B.R.4    McIntosh, J.R.5
  • 20
    • 0023663113 scopus 로고
    • Nuclear reassembly excludes large macromolecules
    • PMID:2443981
    • Swanson JA, McNeil PL. Nuclear reassembly excludes large macromolecules. Science 1987; 238:548-50; PMID:2443981; http://dx.doi.org/10.1126/science. 2443981
    • (1987) Science , vol.238 , pp. 548-550
    • Swanson, J.A.1    McNeil, P.L.2
  • 21
    • 61849128423 scopus 로고    scopus 로고
    • Keeping uracil out of DNA: Physiological role, structure and catalytic mechanism of dUTPases
    • PMID:18837522
    • Vertessy BG, Toth J. Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases. Acc Chem Res 2009; 42:97-106; PMID:18837522; http://dx.doi.org/10.1021/ar800114w
    • (2009) Acc Chem Res , vol.42 , pp. 97-106
    • Vertessy, B.G.1    Toth, J.2
  • 22
    • 84889768217 scopus 로고    scopus 로고
    • Phosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: Structural and mechanistic insights
    • PMID:24311590
    • Rona G, Marfori M, Borsos M, Scheer I, Takacs E, Toth J, Babos F, Magyar A, Erdei A, Bozoky Z, et al. Phosphorylation adjacent to the nuclear localization signal of human dUTPase abolishes nuclear import: structural and mechanistic insights. Acta crystallogr Section D, Biol Crystallogr 2013; 69:2495-505; PMID:24311590; http://dx.doi.org/ 10.1107/S0907444913023354
    • (2013) Acta Crystallogr Section D, Biol Crystallogr , vol.69 , pp. 2495-2505
    • Rona, G.1    Marfori, M.2    Borsos, M.3    Scheer, I.4    Takacs, E.5    Toth, J.6    Babos, F.7    Magyar, A.8    Erdei, A.9    Bozoky, Z.10
  • 24
    • 77952088459 scopus 로고    scopus 로고
    • An overview of Cdk1-controlled targets and processes
    • PMID:20465793
    • Enserink JM, Kolodner RD. An overview of Cdk1-controlled targets and processes. Cell division 2010; 5:11; PMID:20465793; http://dx.doi.org/10.1186/1747-1028-5-11
    • (2010) Cell Division , vol.5 , pp. 11
    • Enserink, J.M.1    Kolodner, R.D.2
  • 25
    • 48449084853 scopus 로고    scopus 로고
    • The Predikin webserver: Improved prediction of protein kinase peptide specificity using structural information
    • PMID:18477637
    • Saunders NF, Kobe B. The Predikin webserver: improved prediction of protein kinase peptide specificity using structural information. Nucl Acids Res 2008; 36:W286-90; PMID:18477637; http://dx.doi.org/ 10.1093/nar/gkn279
    • (2008) Nucl Acids Res , vol.36 , pp. W286-W290
    • Saunders, N.F.1    Kobe, B.2
  • 26
    • 1542284074 scopus 로고    scopus 로고
    • Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6
    • PMID:14993267
    • Geymonat M, Spanos A, Wells GP, Smerdon SJ, Sedgwick SG. Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6. Mol Cell Biol 2004; 24:2277-85; PMID:14993267; http://dx. doi.org/10.1128/MCB.24.6.2277-2285.2004
    • (2004) Mol Cell Biol , vol.24 , pp. 2277-2285
    • Geymonat, M.1    Spanos, A.2    Wells, G.P.3    Smerdon, S.J.4    Sedgwick, S.G.5
  • 27
    • 2442688987 scopus 로고    scopus 로고
    • Regulation of nuclear import by phosphorylation adjacent to nuclear localization signals
    • PMID:14998990
    • Harreman MT, Kline TM, Milford HG, Harben MB, Hodel AE, Corbett AH. Regulation of nuclear import by phosphorylation adjacent to nuclear localization signals. J Biol Chem 2004; 279:20613-21; PMID:14998990; http://dx.doi.org/10.1074/jbc. M401720200
    • (2004) J Biol Chem , vol.279 , pp. 20613-20621
    • Harreman, M.T.1    Kline, T.M.2    Milford, H.G.3    Harben, M.B.4    Hodel, A.E.5    Corbett, A.H.6
  • 28
    • 0028820406 scopus 로고
    • Cell cycle-regulated phosphorylation of Swi6 controls its nuclear localization
    • PMID:8590795
    • Sidorova JM, Mikesell GE, Breeden LL. Cell cycle-regulated phosphorylation of Swi6 controls its nuclear localization. Mol Biol Cell 1995; 6:1641-58; PMID:8590795; http://dx.doi.org/10.1091/mbc.6.12. 1641
    • (1995) Mol Biol Cell , vol.6 , pp. 1641-1658
    • Sidorova, J.M.1    Mikesell, G.E.2    Breeden, L.L.3
  • 29
    • 51649083754 scopus 로고    scopus 로고
    • Design of peptide inhibitors for the importin alpha/beta nuclear import pathway by activity-based profiling
    • PMID:18804031
    • Kosugi S, Hasebe M, Entani T, Takayama S, Tomita M, Yanagawa H. Design of peptide inhibitors for the importin alpha/beta nuclear import pathway by activity-based profiling. Chem Biol 2008; 15:940-9; PMID:18804031; http://dx.doi.org/10.1016/j.chembiol. 2008.07.019
    • (2008) Chem Biol , vol.15 , pp. 940-949
    • Kosugi, S.1    Hasebe, M.2    Entani, T.3    Takayama, S.4    Tomita, M.5    Yanagawa, H.6
  • 32
    • 0030929857 scopus 로고    scopus 로고
    • Identification of a region within the ubiquitin-activating enzyme required for nuclear targeting and phosphorylation
    • PMID:9099746
    • Stephen AG, Trausch-Azar JS, Handley-Gearhart PM, Ciechanover A, Schwartz AL. Identification of a region within the ubiquitin-activating enzyme required for nuclear targeting and phosphorylation. J Biol Chem 1997; 272:10895-903; PMID:9099746; http://dx.doi. org/10.1074/jbc.272.16.10895
    • (1997) J Biol Chem , vol.272 , pp. 10895-10903
    • Stephen, A.G.1    Trausch-Azar, J.S.2    Handley-Gearhart, P.M.3    Ciechanover, A.4    Schwartz, A.L.5
  • 33
    • 78651277063 scopus 로고    scopus 로고
    • Serine 312 phosphorylation is dispensable for wild-type p53 functions in vivo
    • PMID:20671749
    • Lee MK, Tong WM, Wang ZQ, Sabapathy K. Serine 312 phosphorylation is dispensable for wild-type p53 functions in vivo. Cell Death Differ 2010; 18:214-21; PMID:20671749; http://dx.doi.org/10.1038/cdd.2010.90
    • (2010) Cell Death Differ , vol.18 , pp. 214-221
    • Lee, M.K.1    Tong, W.M.2    Wang, Z.Q.3    Sabapathy, K.4
  • 34
    • 0032531934 scopus 로고    scopus 로고
    • Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively
    • PMID:9753728
    • Otterlei M, Haug T, Nagelhus TA, Slupphaug G, Lindmo T, Krokan HE. Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively. Nucl Acids Res 1998; 26:4611-7; PMID:9753728; http:// dx.doi.org/10.1093/nar/26.20.4611
    • (1998) Nucl Acids Res , vol.26 , pp. 4611-4617
    • Otterlei, M.1    Haug, T.2    Nagelhus, T.A.3    Slupphaug, G.4    Lindmo, T.5    Krokan, H.E.6
  • 35
    • 0034694904 scopus 로고    scopus 로고
    • Altered subunit communication in subfamilies of trimeric dUTPases
    • PMID:11118321
    • Fiser A, Vertessy BG. Altered subunit communication in subfamilies of trimeric dUTPases. Biochem Biophys Res Commun 2000; 279:534-42; PMID:11118321; http://dx.doi.org/10.1006/bbrc.2000.3994
    • (2000) Biochem Biophys Res Commun , vol.279 , pp. 534-542
    • Fiser, A.1    Vertessy, B.G.2
  • 36
    • 0037610790 scopus 로고    scopus 로고
    • Catalytic and structural role of the metal ion in dUTP pyrophosphatase
    • PMID:12721364
    • Mustafi D, Bekesi A, Vertessy BG, Makinen MW. Catalytic and structural role of the metal ion in dUTP pyrophosphatase. Proc Nat Acad Sci U S A 2003; 100:5670-5; PMID:12721364; http://dx.doi.org/ 10.1073/pnas.1031504100
    • (2003) Proc Nat Acad Sci U S A , vol.100 , pp. 5670-5675
    • Mustafi, D.1    Bekesi, A.2    Vertessy, B.G.3    Makinen, M.W.4
  • 37
    • 0029874744 scopus 로고    scopus 로고
    • Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site
    • PMID:8604980
    • Vertessy BG, Persson R, Rosengren AM, Zeppezauer M, Nyman PO. Specific derivatization of the active site tyrosine in dUTPase perturbs ligand binding to the active site. Biochem Biophys Res Commun 1996; 219:294-300; PMID:8604980; http://dx.doi.org/ 10.1006/bbrc.1996.0226
    • (1996) Biochem Biophys Res Commun , vol.219 , pp. 294-300
    • Vertessy, B.G.1    Persson, R.2    Rosengren, A.M.3    Zeppezauer, M.4    Nyman, P.O.5
  • 38
    • 40549141791 scopus 로고    scopus 로고
    • Methylene substitution at the alpha-beta bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site
    • PMID:17932923
    • Kovari J, Barabas O, Varga B, Bekesi A, Tolgyesi F, Fidy J, Nagy J, Vertessy BG. Methylene substitution at the alpha-beta bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site. Proteins 2008; 71:308-19; PMID:17932923; http://dx.doi.org/ 10.1002/prot.21757
    • (2008) Proteins , vol.71 , pp. 308-319
    • Kovari, J.1    Barabas, O.2    Varga, B.3    Bekesi, A.4    Tolgyesi, F.5    Fidy, J.6    Nagy, J.7    Vertessy, B.G.8
  • 41
    • 2342441633 scopus 로고    scopus 로고
    • Altered active site flexibility and a structural metalbinding site in eukaryotic dUTPase: KInetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme
    • PMID:14724274
    • Kovari J, Barabas O, Takacs E, Bekesi A, Dubrovay Z, Pongracz V, Zagyva I, Imre T, Szabo P, Vertessy BG. Altered active site flexibility and a structural metalbinding site in eukaryotic dUTPase: kinetic characterization, folding, and crystallographic studies of the homotrimeric Drosophila enzyme. J Biol Chem 2004; 279:17932-44; PMID:14724274; http://dx.doi.org/ 10.1074/jbc.M313643200
    • (2004) J Biol Chem , vol.279 , pp. 17932-17944
    • Kovari, J.1    Barabas, O.2    Takacs, E.3    Bekesi, A.4    Dubrovay, Z.5    Pongracz, V.6    Zagyva, I.7    Imre, T.8    Szabo, P.9    Vertessy, B.G.10
  • 42
    • 33750935665 scopus 로고    scopus 로고
    • Quantitative determination of uracil residues in Escherichia coli DNA: Contribution of ung, dug, and dut genes to uracil avoidance
    • PMID:16908222
    • Lari SU, Chen CY, Vertessy BG, Morre J, Bennett SE. Quantitative determination of uracil residues in Escherichia coli DNA: Contribution of ung, dug, and dut genes to uracil avoidance. DNA Repair 2006; 5:1407-20; PMID:16908222; http://dx.doi.org/10.1016/j. dnarep.2006.06.009
    • (2006) DNA Repair , vol.5 , pp. 1407-1420
    • Lari, S.U.1    Chen, C.Y.2    Vertessy, B.G.3    Morre, J.4    Bennett, S.E.5
  • 43
    • 79961013181 scopus 로고    scopus 로고
    • Cellular response to efficient dUTPase RNAi silencing in stable HeLa cell lines perturbs expression levels of genes involved in thymidylate metabolism
    • PMID:21780905
    • Merenyi G, Kovari J, Toth J, Takacs E, Zagyva I, Erdei A, Vertessy BG. Cellular response to efficient dUTPase RNAi silencing in stable HeLa cell lines perturbs expression levels of genes involved in thymidylate metabolism. Nucleosides Nucleotides Nucleic Acids 2011; 30:369-90; PMID:21780905; http://dx.doi.org/ 10.1080/15257770.2011.582849
    • (2011) Nucleosides Nucleotides Nucleic Acids , vol.30 , pp. 369-390
    • Merenyi, G.1    Kovari, J.2    Toth, J.3    Takacs, E.4    Zagyva, I.5    Erdei, A.6    Vertessy, B.G.7
  • 45
    • 84861438630 scopus 로고    scopus 로고
    • The dUTPase enzyme is essential in Mycobacterium smegmatis
    • PMID:22655049
    • Pecsi I, Hirmondo R, Brown AC, Lopata A, Parish T, Vertessy BG, Toth J. The dUTPase enzyme is essential in Mycobacterium smegmatis. PLoS One 2012; 7: e37461; PMID:22655049; http://dx.doi.org/10.1371/ journal.pone.0037461
    • (2012) PLoS One , vol.7 , pp. e37461
    • Pecsi, I.1    Hirmondo, R.2    Brown, A.C.3    Lopata, A.4    Parish, T.5    Vertessy, B.G.6    Toth, J.7
  • 46
    • 0029979550 scopus 로고    scopus 로고
    • Identification of a consensus cyclindependent kinase phosphorylation site unique to the nuclear form of human deoxyuridine triphosphate nucleotidohydrolase
    • PMID:8631817
    • Ladner RD, Carr SA, Huddleston MJ, McNulty DE, Caradonna SJ. Identification of a consensus cyclindependent kinase phosphorylation site unique to the nuclear form of human deoxyuridine triphosphate nucleotidohydrolase. J Biol Chem 1996; 271:7752-7; PMID:8631817; http://dx.doi.org/10.1074/jbc.271. 13.7752
    • (1996) J Biol Chem , vol.271 , pp. 7752-7757
    • Ladner, R.D.1    Carr, S.A.2    Huddleston, M.J.3    McNulty, D.E.4    Caradonna, S.J.5
  • 47
    • 36349007726 scopus 로고    scopus 로고
    • Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme
    • PMID:17848562
    • Toth J, Varga B, Kovacs M, Malnasi-Csizmadia A, Vertessy BG. Kinetic mechanism of human dUTPase, an essential nucleotide pyrophosphatase enzyme. J Biol Chem 2007; 282:33572-82; PMID:17848562; http:// dx.doi.org/10.1074/jbc.M706230200
    • (2007) J Biol Chem , vol.282 , pp. 33572-33582
    • Toth, J.1    Varga, B.2    Kovacs, M.3    Malnasi-Csizmadia, A.4    Vertessy, B.G.5
  • 48
    • 0037530083 scopus 로고    scopus 로고
    • Identification of sequence determinants of human nuclear dUTPase isoform localization
    • PMID:12799180
    • Tinkelenberg BA, Fazzone W, Lynch FJ, Ladner RD. Identification of sequence determinants of human nuclear dUTPase isoform localization. Exp Cell Res 2003; 287:39-46; PMID:12799180; http://dx.doi.org/ 10.1016/S0014-4827(03)00048-X
    • (2003) Exp Cell Res , vol.287 , pp. 39-46
    • Tinkelenberg, B.A.1    Fazzone, W.2    Lynch, F.J.3    Ladner, R.D.4
  • 49
    • 83755181500 scopus 로고    scopus 로고
    • Nuclear localization of de novo thymidylate biosynthesis pathway is required to prevent uracil accumulation in DNA
    • MacFarlane AJ, Anderson DD, Flodby P, Perry CA, Allen RH, Stabler SP, Stover PJ. Nuclear localization of de novo thymidylate biosynthesis pathway is required to prevent uracil accumulation in DNA. J Biol Chem 2012; 286:44015-22; http://dx.doi.org/ 10.1074/jbc.M111.307629
    • (2012) J Biol Chem , vol.286 , pp. 44015-44022
    • MacFarlane, A.J.1    Anderson, D.D.2    Flodby, P.3    Perry, C.A.4    Allen, R.H.5    Stabler, S.P.6    Stover, P.J.7
  • 50
    • 84863398662 scopus 로고    scopus 로고
    • Competition between sumoylation and ubiquitination of serine hydroxymethyltransferase 1 determines its nuclear localization and its accumulation in the nucleus
    • PMID:22194612
    • Anderson DD, Eom JY, Stover PJ. Competition between sumoylation and ubiquitination of serine hydroxymethyltransferase 1 determines its nuclear localization and its accumulation in the nucleus. J Biol Chem 2012; 287:4790-9; PMID:22194612; http://dx. doi.org/10.1074/jbc.M111.302174
    • (2012) J Biol Chem , vol.287 , pp. 4790-4799
    • Anderson, D.D.1    Eom, J.Y.2    Stover, P.J.3
  • 51
    • 34547101719 scopus 로고    scopus 로고
    • Evidence for small ubiquitin-like modifier-dependent nuclear import of the thymidylate biosynthesis pathway
    • PMID:17446168
    • Woeller CF, Anderson DD, Szebenyi DM, Stover PJ. Evidence for small ubiquitin-like modifier-dependent nuclear import of the thymidylate biosynthesis pathway. J Biol Chem 2007; 282:17623-31; PMID:17446168; http://dx.doi.org/10.1074/jbc.M702526200
    • (2007) J Biol Chem , vol.282 , pp. 17623-17631
    • Woeller, C.F.1    Anderson, D.D.2    Szebenyi, D.M.3    Stover, P.J.4
  • 52
    • 84863421311 scopus 로고    scopus 로고
    • Serine hydroxymethyltransferase anchors de novo thymidylate synthesis pathway to nuclear lamina for DNA synthesis
    • PMID:22235121
    • Anderson DD, Woeller CF, Chiang EP, Shane B, Stover PJ. Serine hydroxymethyltransferase anchors de novo thymidylate synthesis pathway to nuclear lamina for DNA synthesis. J Biol Chem 2012; 287:7051-62; PMID:22235121; http://dx.doi.org/10.1074/jbc.M111. 333120
    • (2012) J Biol Chem , vol.287 , pp. 7051-7062
    • Anderson, D.D.1    Woeller, C.F.2    Chiang, E.P.3    Shane, B.4    Stover, P.J.5
  • 53
    • 78449268395 scopus 로고    scopus 로고
    • Mechanisms of dNTP supply that play an essential role in maintaining genome integrity in eukaryotic cells
    • PMID:20874841
    • Niida H, Shimada M, Murakami H, Nakanishi M. Mechanisms of dNTP supply that play an essential role in maintaining genome integrity in eukaryotic cells. Cancer Sci 2010; 101:2505-9; PMID:20874841; http://dx.doi.org/10.1111/j.1349-7006.2010.01719.x
    • (2010) Cancer Sci , vol.101 , pp. 2505-2509
    • Niida, H.1    Shimada, M.2    Murakami, H.3    Nakanishi, M.4
  • 55
    • 81055155450 scopus 로고    scopus 로고
    • Regulatory networks integrating cell cycle control with DNA damage checkpoints and double-strand break repair
    • Langerak P, Russell P. Regulatory networks integrating cell cycle control with DNA damage checkpoints and double-strand break repair. Philos Trans R Soc Lond B Biol Sci 2012; 366:3562-71; http://dx.doi.org/ 10.1098/rstb.2011.0070
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.366 , pp. 3562-3571
    • Langerak, P.1    Russell, P.2
  • 57
    • 77952294068 scopus 로고    scopus 로고
    • The BRCA-1 binding protein BRAP2 is a novel, negative regulator of nuclear import of viral proteins, dependent on phosphorylation flanking the nuclear localization signal
    • PMID:20040518
    • Fulcher AJ, Roth DM, Fatima S, Alvisi G, Jans DA. The BRCA-1 binding protein BRAP2 is a novel, negative regulator of nuclear import of viral proteins, dependent on phosphorylation flanking the nuclear localization signal. FASEB J 2010; 24:1454-66; PMID:20040518; http://dx.doi.org/10.1096/fj.09-136564
    • (2010) FASEB J , vol.24 , pp. 1454-1466
    • Fulcher, A.J.1    Roth, D.M.2    Fatima, S.3    Alvisi, G.4    Jans, D.A.5
  • 58
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • PMID:22102590
    • Uniprot C. Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucl Acids Res 2012; 40:D71-5; PMID:22102590; http://dx.doi.org/ 10.1093/nar/gkr981
    • (2012) Nucl Acids Res , vol.40 , pp. D71-D75
    • Uniprot, C.1
  • 59
    • 58649104919 scopus 로고    scopus 로고
    • Six classes of nuclear localization signals specific to different binding grooves of importin alpha
    • PMID:19001369
    • Kosugi S, Hasebe M, Matsumura N, Takashima H, Miyamoto-Sato E, Tomita M, Yanagawa H. Six classes of nuclear localization signals specific to different binding grooves of importin alpha. J Biol Chem 2009; 284:478-85; PMID:19001369; http://dx.doi.org/ 10.1074/jbc.M807017200
    • (2009) J Biol Chem , vol.284 , pp. 478-485
    • Kosugi, S.1    Hasebe, M.2    Matsumura, N.3    Takashima, H.4    Miyamoto-Sato, E.5    Tomita, M.6    Yanagawa, H.7
  • 61
    • 0032936125 scopus 로고    scopus 로고
    • Mapping of nuclear localization signals by simultaneous fusion to green fluorescent protein and to beta-galactosidase
    • PMID:10337476
    • Sorg G, Stamminger T. Mapping of nuclear localization signals by simultaneous fusion to green fluorescent protein and to beta-galactosidase. Biotechniques 1999; 26:858-62; PMID:10337476
    • (1999) Biotechniques , vol.26 , pp. 858-862
    • Sorg, G.1    Stamminger, T.2
  • 62
    • 78651277460 scopus 로고    scopus 로고
    • PHOSIDA 2011: The posttranslational modification database
    • PMID:21081558
    • Gnad F, Gunawardena J, Mann M. PHOSIDA 2011: the posttranslational modification database. Nucl Acids Res 2011; 39:D253-60; PMID:21081558; http://dx. doi.org/10.1093/nar/gkq1159
    • (2011) Nucl Acids Res , vol.39 , pp. D253-D260
    • Gnad, F.1    Gunawardena, J.2    Mann, M.3
  • 63
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): Management, structural and evolutionary investigation, and prediction of phosphosites
    • PMID:18039369
    • Gnad F, Ren S, Cox J, Olsen JV, Macek B, Oroshi M, Mann M. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol 2007; 8: R250; PMID:18039369; http://dx.doi.org/10.1186/ gb-2007-8-11-r250
    • (2007) Genome Biol , vol.8 , pp. R250
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.V.4    Macek, B.5    Oroshi, M.6    Mann, M.7
  • 64
    • 47749141560 scopus 로고    scopus 로고
    • ATR: An essential regulator of genome integrity
    • PMID:18594563
    • Cimprich KA, Cortez D. ATR: an essential regulator of genome integrity. Nat Rev Mol Cell Biol 2008; 9:616-27; PMID:18594563; http://dx.doi.org/10.1038/ nrm2450
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 616-627
    • Cimprich, K.A.1    Cortez, D.2
  • 65
    • 34249950879 scopus 로고    scopus 로고
    • Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response
    • PMID:17525342
    • Kim H, Chen J, Yu X. Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage response. Science 2007; 316:1202-5; PMID:17525342; http://dx.doi. org/10.1126/science.1139621
    • (2007) Science , vol.316 , pp. 1202-1205
    • Kim, H.1    Chen, J.2    Yu, X.3
  • 67
    • 48549085044 scopus 로고    scopus 로고
    • The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A
    • PMID:18593899
    • Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachinsky I, Levine AS, Rapic-Otrin V. The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A. Cancer Res 2008; 68:5014-22; PMID:18593899; http://dx.doi.org/10.1158/0008-5472. CAN-07-6162
    • (2008) Cancer Res , vol.68 , pp. 5014-5022
    • Guerrero-Santoro, J.1    Kapetanaki, M.G.2    Hsieh, C.L.3    Gorbachinsky, I.4    Levine, A.S.5    Rapic-Otrin, V.6
  • 68
    • 71049180608 scopus 로고    scopus 로고
    • Complementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2
    • PMID:19505873
    • Ku WC, Chiu SK, Chen YJ, Huang HH, Wu WG. Complementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2. Mol Cell Proteomics 2009; 8:2034-50; PMID:19505873; http://dx.doi.org/10.1074/mcp. M900013-MCP200
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2034-2050
    • Ku, W.C.1    Chiu, S.K.2    Chen, Y.J.3    Huang, H.H.4    Wu, W.G.5
  • 69
    • 78751611793 scopus 로고    scopus 로고
    • Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation
    • PMID:21131905
    • Jin Q, Yu LR, Wang L, Zhang Z, Kasper LH, Lee JE, Wang C, Brindle PK, Dent SY, Ge K. Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation. EMBO J 2011; 30:249-62; PMID:21131905; http://dx.doi.org/10.1038/emboj.2010.318
    • (2011) EMBO J , vol.30 , pp. 249-262
    • Jin, Q.1    Yu, L.R.2    Wang, L.3    Zhang, Z.4    Kasper, L.H.5    Lee, J.E.6    Wang, C.7    Brindle, P.K.8    Dent, S.Y.9    Ge, K.10
  • 70
    • 70249118941 scopus 로고    scopus 로고
    • DNA damage signalling recruits RREB-1 to the p53 tumour suppressor promoter
    • PMID:19558368
    • Liu H, Hew HC, Lu ZG, Yamaguchi T, Miki Y, Yoshida K. DNA damage signalling recruits RREB-1 to the p53 tumour suppressor promoter. Biochem J 2009; 422:543-51; PMID:19558368; http://dx.doi.org/ 10.1042/BJ20090342
    • (2009) Biochem J , vol.422 , pp. 543-551
    • Liu, H.1    Hew, H.C.2    Lu, Z.G.3    Yamaguchi, T.4    Miki, Y.5    Yoshida, K.6
  • 72
    • 2942612219 scopus 로고    scopus 로고
    • P300/CBP and cancer
    • PMID:15156177
    • Iyer NG, Ozdag H, Caldas C. p300/CBP and cancer. Oncogene 2004; 23:4225-31; PMID:15156177; http://dx.doi.org/10.1038/sj.onc.1207118
    • (2004) Oncogene , vol.23 , pp. 4225-4231
    • Iyer, N.G.1    Ozdag, H.2    Caldas, C.3
  • 73
    • 80052557419 scopus 로고    scopus 로고
    • Transcription factor AP4 modulates reversible and epigenetic silencing of the Cd4 gene
    • PMID:21873191
    • Egawa T, Littman DR. Transcription factor AP4 modulates reversible and epigenetic silencing of the Cd4 gene. Proc Nat Acad Sci U S A 2011; 108:14873-8; PMID:21873191; http://dx.doi.org/10.1073/pnas. 1112293108
    • (2011) Proc Nat Acad Sci U S A , vol.108 , pp. 14873-14878
    • Egawa, T.1    Littman, D.R.2
  • 74
    • 33744952170 scopus 로고    scopus 로고
    • Transcriptional repression of human immunodeficiency virus type 1 by AP-4
    • PMID:16540471
    • Imai K, Okamoto T. Transcriptional repression of human immunodeficiency virus type 1 by AP-4. J Biol Chem 2006; 281:12495-505; PMID:16540471; http://dx.doi.org/10.1074/jbc.M511773200
    • (2006) J Biol Chem , vol.281 , pp. 12495-12505
    • Imai, K.1    Okamoto, T.2
  • 75
    • 77954954525 scopus 로고    scopus 로고
    • The NoRC complex mediates the heterochromatin formation and stability of silent rRNA genes and centromeric repeats
    • PMID:20168299
    • Guetg C, Lienemann P, Sirri V, Grummt I, Hernan-dez-Verdun D, Hottiger MO, Fussenegger M, Santoro R. The NoRC complex mediates the heterochromatin formation and stability of silent rRNA genes and centromeric repeats. EMBO J 2010; 29:2135-46; PMID:20168299; http://dx.doi.org/10.1038/emboj. 2010.17
    • (2010) EMBO J , vol.29 , pp. 2135-2146
    • Guetg, C.1    Lienemann, P.2    Sirri, V.3    Grummt, I.4    Hernan-dez-Verdun, D.5    Hottiger, M.O.6    Fussenegger, M.7    Santoro, R.8
  • 76
    • 0035801407 scopus 로고    scopus 로고
    • NoRC-a novel member of mammalian ISWI-containing chromatin remodeling machines
    • PMID:11532953
    • Strohner R, Nemeth A, Jansa P, Hofmann-Rohrer U, Santoro R, Langst G, Grummt I. NoRC-a novel member of mammalian ISWI-containing chromatin remodeling machines. EMBO J 2001; 20:4892-900; PMID:11532953; http://dx.doi.org/10.1093/emboj/20. 17.4892
    • (2001) EMBO J , vol.20 , pp. 4892-4900
    • Strohner, R.1    Nemeth, A.2    Jansa, P.3    Hofmann-Rohrer, U.4    Santoro, R.5    Langst, G.6    Grummt, I.7
  • 77
    • 27144554969 scopus 로고    scopus 로고
    • Ubiquitin ligase component Cul4 associates with Clr4 histone methyltransferase to assemble heterochromatin
    • PMID:16127433
    • Jia S, Kobayashi R, Grewal SI. Ubiquitin ligase component Cul4 associates with Clr4 histone methyltransferase to assemble heterochromatin. Nat Cell Biol 2005; 7:1007-13; PMID:16127433; http://dx.doi.org/ 10.1038/ncb1300
    • (2005) Nat Cell Biol , vol.7 , pp. 1007-1013
    • Jia, S.1    Kobayashi, R.2    Grewal, S.I.3
  • 79
    • 1642523744 scopus 로고    scopus 로고
    • Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells
    • PMID:14684736
    • Yang L, Li N, Wang C, Yu Y, Yuan L, Zhang M, Cao X. Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells. J Biol Chem 2004; 279:11639-48; PMID:14684736; http://dx.doi.org/10.1074/jbc.M312895200
    • (2004) J Biol Chem , vol.279 , pp. 11639-11648
    • Yang, L.1    Li, N.2    Wang, C.3    Yu, Y.4    Yuan, L.5    Zhang, M.6    Cao, X.7
  • 80
    • 70450225328 scopus 로고    scopus 로고
    • Characterization of nuclear localization signal in the N terminus of CUL4B and its essential role in cyclin E degradation and cell cycle progression
    • PMID:19801544
    • Zou Y, Mi J, Cui J, Lu D, Zhang X, Guo C, Gao G, Liu Q, Chen B, Shao C, et al. Characterization of nuclear localization signal in the N terminus of CUL4B and its essential role in cyclin E degradation and cell cycle progression. J Biol Chem 2009; 284:33320-32; PMID:19801544; http://dx.doi.org/10.1074/jbc. M109.050427
    • (2009) J Biol Chem , vol.284 , pp. 33320-33332
    • Zou, Y.1    Mi, J.2    Cui, J.3    Lu, D.4    Zhang, X.5    Guo, C.6    Gao, G.7    Liu, Q.8    Chen, B.9    Shao, C.10
  • 82
    • 33645309411 scopus 로고    scopus 로고
    • Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors Dacapo/p27Kip1 and cyclin E degradation
    • PMID:16322693
    • Higa LA, Yang X, Zheng J, Banks D, Wu M, Ghosh P, Sun H, Zhang H. Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors Dacapo/p27Kip1 and cyclin E degradation. Cell Cycle 2006; 5:71-7; PMID:16322693; http://dx.doi.org/10.4161/cc.5.1.2266
    • (2006) Cell Cycle , vol.5 , pp. 71-77
    • Higa, L.A.1    Yang, X.2    Zheng, J.3    Banks, D.4    Wu, M.5    Ghosh, P.6    Sun, H.7    Zhang, H.8
  • 83
    • 34249794559 scopus 로고    scopus 로고
    • Overexpression of cyclin L2 induces apoptosis and cell-cycle arrest in human lung cancer cells
    • PMID:17543181
    • Li HL, Wang TS, Li XY, Li N, Huang DZ, Chen Q, Ba Y. Overexpression of cyclin L2 induces apoptosis and cell-cycle arrest in human lung cancer cells. Chin Med J (Engl) 2007; 120:905-9; PMID:17543181
    • (2007) Chin Med J (Engl) , vol.120 , pp. 905-909
    • Li, H.L.1    Wang, T.S.2    Li, X.Y.3    Li, N.4    Huang, D.Z.5    Chen, Q.6    Ba, Y.7
  • 84
    • 44449116119 scopus 로고    scopus 로고
    • Tlx3 exerts context-dependent transcriptional regulation and promotes neuronal differentiation from embryonic stem cells
    • PMID:18391221
    • Kondo T, Sheets PL, Zopf DA, Aloor HL, Cummins TR, Chan RJ, Hashino E. Tlx3 exerts context-dependent transcriptional regulation and promotes neuronal differentiation from embryonic stem cells. Proc Nat Acad Sci U S A 2008; 105:5780-5; PMID:18391221; http://dx.doi.org/10.1073/pnas.0708704105
    • (2008) Proc Nat Acad Sci U S A , vol.105 , pp. 5780-5785
    • Kondo, T.1    Sheets, P.L.2    Zopf, D.A.3    Aloor, H.L.4    Cummins, T.R.5    Chan, R.J.6    Hashino, E.7
  • 85
    • 82755161872 scopus 로고    scopus 로고
    • Nuclear lamins and laminopathies
    • PMID:21953297
    • Worman HJ. Nuclear lamins and laminopathies. J Pathol 2011; 226:316-25; PMID:21953297; http://dx. doi.org/10.1002/path.2999
    • (2011) J Pathol , vol.226 , pp. 316-325
    • Worman, H.J.1
  • 86
    • 79957654428 scopus 로고    scopus 로고
    • The lamin protein family
    • PMID:21639948
    • Dittmer TA, Misteli T. The lamin protein family. Genome Biol 2011; 12:222; PMID:21639948; http:// dx.doi.org/10.1186/gb-2011-12-5-222
    • (2011) Genome Biol , vol.12 , pp. 222
    • Dittmer, T.A.1    Misteli, T.2


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