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Volumn 25, Issue 10, 2014, Pages 1641-1652

Nucleophosmin modulates stability, activity, and nucleolar accumulation of base excision repair proteins

Author keywords

[No Author keywords available]

Indexed keywords

APYRIMIDINIC ENDONUCLEASE 1; CISPLATIN; DEOXYRIBONUCLEASE I; ENDONUCLEASE; NUCLEOPHOSMIN; PROTEIN P53; UNCLASSIFIED DRUG; APEX1 PROTEIN, MOUSE; CROSS LINKING REAGENT; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA LIGASE (ATP); DOXYCYCLINE; FEN1 PROTEIN, MOUSE; FLAP ENDONUCLEASE; NUCLEAR PROTEIN; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; SMALL INTERFERING RNA;

EID: 84901236223     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-12-0717     Document Type: Article
Times cited : (62)

References (45)
  • 1
    • 0037200841 scopus 로고    scopus 로고
    • Induction of metallothionein by zinc protects from daunorubicin toxicity in rats
    • Ali MM, Frei E, Straub J, Breuer A, Wiessler M (2002). Induction of metallothionein by zinc protects from daunorubicin toxicity in rats. Toxicology 179, 85-93.
    • (2002) Toxicology , vol.179 , pp. 85-93
    • Ali, M.M.1    Frei, E.2    Straub, J.3    Breuer, A.4    Wiessler, M.5
  • 2
    • 84892932423 scopus 로고    scopus 로고
    • Emerging roles of the nucleolus in regulating the dna damage response: The non-canonical dna repair enzyme ape1/ref-1 as a paradigmatical example
    • Antoniali G, Lirussi L, Poletto M, Tell G (2014). Emerging roles of the nucleolus in regulating the DNA damage response: the non-canonical DNA repair enzyme APE1/Ref-1 as a paradigmatical example. Antioxid Redox Signal 20, 621-639.
    • (2014) Antioxid Redox Signal , vol.20 , pp. 621-639
    • Antoniali, G.1    Lirussi, L.2    Poletto, M.3    Tell, G.4
  • 3
    • 38549104216 scopus 로고    scopus 로고
    • A non-Tumor suppressor role for basal p19arf in maintaining nucleolar structure and function
    • Apicelli AJ et al. (2008). A non-Tumor suppressor role for basal p19ARF in maintaining nucleolar structure and function. Mol Cell Biol 28, 1068-1080.
    • (2008) Mol Cell Biol , vol.28 , pp. 1068-1080
    • Apicelli, A.J.1
  • 5
    • 77951248778 scopus 로고    scopus 로고
    • Chemotherapeutic drugs inhibit ribosome biogenesis at various levels
    • Burger K et al. (2010). Chemotherapeutic drugs inhibit ribosome biogenesis at various levels. J Biol Chem 16, 12416-12425.
    • (2010) J Biol Chem , vol.16 , pp. 12416-12425
    • Burger, K.1
  • 6
    • 64049110265 scopus 로고    scopus 로고
    • Ubiquitination of mammalian ap endonuclease (ape1) regulated by the p53-mdm2 signaling pathway
    • Busso CS, Iwakuma T, Izumi T (2009). Ubiquitination of mammalian AP endonuclease (APE1) regulated by the p53-MDM2 signaling pathway. Oncogene 28, 1616-1625.
    • (2009) Oncogene , vol.28 , pp. 1616-1625
    • Busso, C.S.1    Iwakuma, T.2    Izumi, T.3
  • 8
    • 79958273714 scopus 로고    scopus 로고
    • Nucleophosmin and its complex network: A possible therapeutic target in hematological diseases
    • Colombo E, Alcalay M, Pelicci PG (2011). Nucleophosmin and its complex network: a possible therapeutic target in hematological diseases. Oncogene 30, 2595-2609.
    • (2011) Oncogene , vol.30 , pp. 2595-2609
    • Colombo, E.1    Alcalay, M.2    Pelicci, P.G.3
  • 10
    • 61849119563 scopus 로고    scopus 로고
    • Nucleolar targeting: The hub of the matter
    • Emmott E, Hiscox JA (2009). Nucleolar targeting: the hub of the matter. EMBO Rep 10, 231-238.
    • (2009) EMBO Rep , vol.10 , pp. 231-238
    • Emmott, E.1    Hiscox, J.A.2
  • 11
    • 78650501028 scopus 로고    scopus 로고
    • Critical lysine residues within the overlooked n-Terminal domain of human ape1 regulate its biological functions
    • Fantini D et al. (2010). Critical lysine residues within the overlooked N-Terminal domain of human APE1 regulate its biological functions. Nucleic Acids Res 38, 8239-8256.
    • (2010) Nucleic Acids Res , vol.38 , pp. 8239-8256
    • Fantini, D.1
  • 12
    • 79953720878 scopus 로고    scopus 로고
    • The multifunctional protein nucleophosmin (npm1) is a human linker histone h1 chaperone
    • Gadad SS et al. (2011). The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone. Biochemistry 50, 2780-2789.
    • (2011) Biochemistry , vol.50 , pp. 2780-2789
    • Gadad, S.S.1
  • 14
    • 46149122987 scopus 로고    scopus 로고
    • Nucleolar localization and dynamic roles of flap endonuclease 1 in ribosomal dna replication and damage repair
    • Guo Z, Qian L, Liu R, Dai H, Zhou M, Zheng L, Shen B (2008). Nucleolar localization and dynamic roles of flap endonuclease 1 in ribosomal DNA replication and damage repair. Mol Cell Biol 28, 4310-4319.
    • (2008) Mol Cell Biol , vol.28 , pp. 4310-4319
    • Guo, Z.1    Qian, L.2    Liu, R.3    Dai, H.4    Zhou, M.5    Zheng, L.6    Shen, B.7
  • 15
    • 0028786597 scopus 로고
    • The ribonuclease activity of nucleolar protein b23
    • Herrera JE, Savkur R, Olson MO (1995). The ribonuclease activity of nucleolar protein B23. Nucleic Acids Res 23, 3974-3979.
    • (1995) Nucleic Acids Res , vol.23 , pp. 3974-3979
    • Herrera, J.E.1    Savkur, R.2    Olson, M.O.3
  • 16
    • 84872812804 scopus 로고    scopus 로고
    • The human base excision repair enzyme smug1 directly interacts with dkc1 and contributes to rna quality control
    • Jobert L, Skjeldam HK, Dalhus B, Galashevskaya A, Vågbø CB, Bjørås M, Nilsen H (2013). The human base excision repair enzyme SMUG1 directly interacts with DKC1 and contributes to RNA quality control. Mol Cell 49, 339-345.
    • (2013) Mol Cell , vol.49 , pp. 339-345
    • Jobert, L.1    Skjeldam, H.K.2    Dalhus, B.3    Galashevskaya, A.4    Vågbø, C.B.5    Bjørås, M.6    Nilsen, H.7
  • 17
    • 77956274850 scopus 로고    scopus 로고
    • Recruitment of phosphorylated npm1 to sites of dna damage through rnf8-dependent ubiquitin conjugates
    • Koike A, Nishikawa H, Wu W, Okada Y, Venkitaraman AR, Ohta T (2010). Recruitment of phosphorylated NPM1 to sites of DNA damage through RNF8-dependent ubiquitin conjugates. Cancer Res 70, 6746-6756.
    • (2010) Cancer Res , vol.70 , pp. 6746-6756
    • Koike, A.1    Nishikawa, H.2    Wu, W.3    Okada, Y.4    Venkitaraman, A.R.5    Ohta, T.6
  • 19
    • 84877923913 scopus 로고    scopus 로고
    • Evidence for base excision repair processing of dna interstrand crosslinks
    • Kothandapani A, Patrick SM (2013). Evidence for base excision repair processing of DNA interstrand crosslinks. Mutat Res 743-744, 44-52.
    • (2013) Mutat Res , vol.743-744 , pp. 44-52
    • Kothandapani, A.1    Patrick, S.M.2
  • 21
    • 2342491487 scopus 로고    scopus 로고
    • Nucleolar protein npm interacts with hdm2 and protects tumor suppressor protein p53 from hdm2-mediated degradation
    • Kurki S, Peltonen K, Latonen L, Kiviharju TM, Ojala PM, Meek D, Laiho M (2004). Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation. Cancer Cell 5, 465-475.
    • (2004) Cancer Cell , vol.5 , pp. 465-475
    • Kurki, S.1    Peltonen, K.2    Latonen, L.3    Kiviharju, T.M.4    Ojala, P.M.5    Meek, D.6    Laiho, M.7
  • 22
    • 33751545937 scopus 로고    scopus 로고
    • Nucleophosmin and human cancer
    • Lim MJ, Wang XW (2006). Nucleophosmin and human cancer. Cancer Detect Prev 30, 481-490.
    • (2006) Cancer Detect Prev , vol.30 , pp. 481-490
    • Lim, M.J.1    Wang, X.W.2
  • 23
    • 84867479746 scopus 로고    scopus 로고
    • Nucleolar accumulation of ape1 depends on charged lysine residues that undergo acetylation upon genotoxic stress and modulate its ber activity in cells
    • Lirussi L et al. (2012). Nucleolar accumulation of APE1 depends on charged lysine residues that undergo acetylation upon genotoxic stress and modulate its BER activity in cells. Mol Biol Cell 23, 4079-4096.
    • (2012) Mol Biol Cell , vol.23 , pp. 4079-4096
    • Lirussi, L.1
  • 24
    • 84876738157 scopus 로고    scopus 로고
    • A novel interaction of nucleophosmin with bcl2-Associated x protein regulating death evasion and drug sensitivity in human hepatoma cells
    • Lo SJ et al. (2013). A novel interaction of nucleophosmin with BCL2-Associated X protein regulating death evasion and drug sensitivity in human hepatoma cells. Hepatology 57, 1893-1905.
    • (2013) Hepatology , vol.57 , pp. 1893-1905
    • Lo, S.J.1
  • 26
    • 14044273481 scopus 로고    scopus 로고
    • Parp-1 and parp-2 interact with nucleophosmin/b23 and accumulate in transcriptionally active nucleoli
    • Meder VS, Boeglin M, de Murcia G, Schreiber V (2005). PARP-1 and PARP-2 interact with nucleophosmin/B23 and accumulate in transcriptionally active nucleoli. J Cell Sci 118, 211-222.
    • (2005) J Cell Sci , vol.118 , pp. 211-222
    • Meder, V.S.1    Boeglin, M.2    De Murcia, G.3    Schreiber, V.4
  • 27
    • 84855871792 scopus 로고    scopus 로고
    • Ubiquitin ligase ubr3 regulates cellular levels of the essential dna repair protein ape1 and is required for genome stability
    • Meisenberg C et al. (2011). Ubiquitin ligase UBR3 regulates cellular levels of the essential DNA repair protein APE1 and is required for genome stability. Nucleic Acids Res 40, 701-711.
    • (2011) Nucleic Acids Res , vol.40 , pp. 701-711
    • Meisenberg, C.1
  • 28
    • 15744362987 scopus 로고    scopus 로고
    • Actinomycin d induces histone gamma-h2ax foci and complex formation of gamma-h2ax with ku70 and nuclear dna helicase ii
    • Mischo HE, Hemmerich P, Grosse F, Zhang S (2005). Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II. J Biol Chem 280, 9586-9594.
    • (2005) J Biol Chem , vol.280 , pp. 9586-9594
    • Mischo, H.E.1    Hemmerich, P.2    Grosse, F.3    Zhang, S.4
  • 30
    • 43249087852 scopus 로고    scopus 로고
    • Transcription regulation of the rrna gene by a multifunctional nucleolar protein, b23/nucleophosmin, through its histone chaperone activity
    • Murano K, Okuwaki M, Hisaoka M, Nagata K (2008). Transcription regulation of the rRNA gene by a multifunctional nucleolar protein, B23/nucleophosmin, through its histone chaperone activity. Mol Cell Biol 28, 3114-3126.
    • (2008) Mol Cell Biol , vol.28 , pp. 3114-3126
    • Murano, K.1    Okuwaki, M.2    Hisaoka, M.3    Nagata, K.4
  • 31
  • 32
    • 84876730678 scopus 로고    scopus 로고
    • Co-ordination of base excision repair and genome stability
    • Parsons JL, Dianov GL (2013). Co-ordination of base excision repair and genome stability. DNA Repair (Amst) 12, 326-333.
    • (2013) DNA Repair (Amst , vol.12 , pp. 326-333
    • Parsons, J.L.1    Dianov, G.L.2
  • 33
    • 39549106043 scopus 로고    scopus 로고
    • Chip-mediated degradation and dna damage-dependent stabilization regulate base excision repair proteins
    • Parsons JL, Tait PS, Finch D, Dianova II, Allinson SL, Dianov GL (2008). CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins. Mol Cell 29, 477-487.
    • (2008) Mol Cell , vol.29 , pp. 477-487
    • Parsons, J.L.1    Tait, P.S.2    Finch, D.3    Dianova, I.I.4    Allinson, S.L.5    Dianov, G.L.6
  • 34
    • 84555178744 scopus 로고    scopus 로고
    • In vivo run-on assays to monitor nascent precursor rna transcripts
    • Percipalle P, Louvet E (2012). In vivo run-on assays to monitor nascent precursor RNA transcripts. Methods Mol Biol 809, 519-533.
    • (2012) Methods Mol Biol , vol.809 , pp. 519-533
    • Percipalle, P.1    Louvet, E.2
  • 35
    • 59349083787 scopus 로고    scopus 로고
    • Delocalization of nucleolar poly(adp-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to dna damage
    • Rancourt A, Satoh MS (2009). Delocalization of nucleolar poly(ADP-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to DNA damage. DNA Repair (Amst) 8, 286-297.
    • (2009) DNA Repair (Amst , vol.8 , pp. 286-297
    • Rancourt, A.1    Satoh, M.S.2
  • 36
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to dna damage and other stresses
    • Rubbi CP, Milner J (2003). Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses. EMBO J 22, 6068-6077.
    • (2003) EMBO J , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 37
    • 80054111106 scopus 로고    scopus 로고
    • The novel chemical entity ytr107 inhibits recruitment of nucleophosmin to sites of dna damage, suppressing repair of dna double-strand breaks and enhancing radiosensitization
    • Sekhar KR et al. (2011). The novel chemical entity YTR107 inhibits recruitment of nucleophosmin to sites of DNA damage, suppressing repair of DNA double-strand breaks and enhancing radiosensitization. Clin Cancer Res 17, 6490-6499.
    • (2011) Clin Cancer Res , vol.17 , pp. 6490-6499
    • Sekhar, K.R.1
  • 39
    • 63049121360 scopus 로고    scopus 로고
    • Ape1/ref-1 interacts with npm1 within nucleoli and plays a role in the rrna quality control process
    • Vascotto C et al. (2009). APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process. Mol Cell Biol 29, 1834-1854.
    • (2009) Mol Cell Biol , vol.29 , pp. 1834-1854
    • Vascotto, C.1
  • 41
    • 0033199168 scopus 로고    scopus 로고
    • P53 selective and nonselective replication of an e1b-deleted adenovirus in hepatocellular carcinoma
    • Vollmer CM et al. (1999). p53 selective and nonselective replication of an E1B-deleted adenovirus in hepatocellular carcinoma. Cancer Res 59, 4369-4374.
    • (1999) Cancer Res , vol.59 , pp. 4369-4374
    • Vollmer, C.M.1
  • 43
    • 0037137873 scopus 로고    scopus 로고
    • Involvement of nucleophosmin/b23 in the response of hela cells to uv irradiation
    • Wu MH, Chang JH, Chou CC, Yung BY (2002). Involvement of nucleophosmin/B23 in the response of HeLa cells to UV irradiation. Int J Cancer 97, 297-305.
    • (2002) Int J Cancer , vol.97 , pp. 297-305
    • Wu, M.H.1    Chang, J.H.2    Chou, C.C.3    Yung, B.Y.4
  • 44
    • 0026344260 scopus 로고
    • Analysis of the p53 gene in human uterine carcinoma cell lines
    • Yaginuma Y, Westphal H (1991). Analysis of the p53 gene in human uterine carcinoma cell lines. Cancer Res 51, 6506-6509.
    • (1991) Cancer Res , vol.51 , pp. 6506-6509
    • Yaginuma, Y.1    Westphal, H.2


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