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Volumn 114, Issue 5, 2017, Pages 1045-1050

Human NF-κB repressing factor acts as a stress-regulated switch for ribosomal RNA processing and nucleolar homeostasis surveillance

Author keywords

Heat shock factor 1; NF kappaB; Nucleolus; Proteotoxic stress; rRNA processing

Indexed keywords

BORTEZOMIB; DNA DIRECTED RNA POLYMERASE; EXORIBONUCLEASE; HEAT SHOCK PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; NUCLEAR FACTOR KAPPA B REPRESSING FACTOR; RIBOSOME DNA; RIBOSOME RNA; THAPSIGARGIN; TUNICAMYCIN; UNCLASSIFIED DRUG; DACTINOMYCIN; DNA; HEAT SHOCK TRANSCRIPTION FACTOR; HSF1 PROTEIN, HUMAN; HYBRID PROTEIN; NKRF PROTEIN, HUMAN; REPRESSOR PROTEIN;

EID: 85010931757     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1616112114     Document Type: Article
Times cited : (34)

References (39)
  • 1
    • 84930746830 scopus 로고    scopus 로고
    • The biology of proteostasis in aging and disease
    • Labbadia J, Morimoto RI (2015) The biology of proteostasis in aging and disease. Annu Rev Biochem 84:435-464.
    • (2015) Annu Rev Biochem , vol.84 , pp. 435-464
    • Labbadia, J.1    Morimoto, R.I.2
  • 2
    • 84901012110 scopus 로고    scopus 로고
    • How the nucleus copes with proteotoxic stress
    • Shibata Y, Morimoto RI (2014) How the nucleus copes with proteotoxic stress. Curr Biol 24(10):R463-R474.
    • (2014) Curr Biol , vol.24 , Issue.10 , pp. R463-R474
    • Shibata, Y.1    Morimoto, R.I.2
  • 3
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • Akerfelt M, Morimoto RI, Sistonen L (2010) Heat shock factors: Integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11(8):545-555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.8 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 4
    • 84956903958 scopus 로고    scopus 로고
    • Molecular basis of HSF regulation
    • Nakai A (2016) Molecular basis of HSF regulation. Nat Struct Mol Biol 23(2):93-95.
    • (2016) Nat Struct Mol Biol , vol.23 , Issue.2 , pp. 93-95
    • Nakai, A.1
  • 5
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • Trinklein ND, Murray JI, Hartman SJ, Botstein D, Myers RM (2004) The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol Biol Cell 15(3):1254-1261.
    • (2004) Mol Biol Cell , vol.15 , Issue.3 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 6
    • 77951596453 scopus 로고    scopus 로고
    • AIRAP, a new human heat shock gene regulated by heat shock factor 1
    • Rossi A, et al. (2010) AIRAP, a new human heat shock gene regulated by heat shock factor 1. J Biol Chem 285(18):13607-13615.
    • (2010) J Biol Chem , vol.285 , Issue.18 , pp. 13607-13615
    • Rossi, A.1
  • 7
    • 33747875267 scopus 로고    scopus 로고
    • Targeting the heat shock factor 1 by RNA interference: A potent tool to enhance hyperthermochemotherapy efficacy in cervical cancer
    • Rossi A, Ciafrè S, Balsamo M, Pierimarchi P, Santoro MG (2006) Targeting the heat shock factor 1 by RNA interference: A potent tool to enhance hyperthermochemotherapy efficacy in cervical cancer. Cancer Res 66(15):7678-7685.
    • (2006) Cancer Res , vol.66 , Issue.15 , pp. 7678-7685
    • Rossi, A.1    Ciafrè, S.2    Balsamo, M.3    Pierimarchi, P.4    Santoro, M.G.5
  • 8
    • 84858718448 scopus 로고    scopus 로고
    • NF-κB and the link between inflammation and cancer
    • DiDonato JA, Mercurio F, Karin M (2012) NF-κB and the link between inflammation and cancer. Immunol Rev 246(1):379-400.
    • (2012) Immunol Rev , vol.246 , Issue.1 , pp. 379-400
    • DiDonato, J.A.1    Mercurio, F.2    Karin, M.3
  • 9
    • 0038605236 scopus 로고    scopus 로고
    • NF-kappaB and virus infection: Who controls whom
    • Santoro MG, Rossi A, Amici C (2003) NF-kappaB and virus infection: Who controls whom. EMBO J 22(11):2552-2560.
    • (2003) EMBO J , vol.22 , Issue.11 , pp. 2552-2560
    • Santoro, M.G.1    Rossi, A.2    Amici, C.3
  • 10
    • 0033570917 scopus 로고    scopus 로고
    • Constitutive silencing of IFN-beta promoter is mediated by NRF (NF-kappaB-repressing factor), a nuclear inhibitor of NF-kappaB
    • Nourbakhsh M, Hauser H (1999) Constitutive silencing of IFN-beta promoter is mediated by NRF (NF-kappaB-repressing factor), a nuclear inhibitor of NF-kappaB. EMBO J 18(22):6415-6425.
    • (1999) EMBO J , vol.18 , Issue.22 , pp. 6415-6425
    • Nourbakhsh, M.1    Hauser, H.2
  • 11
    • 0037195139 scopus 로고    scopus 로고
    • Identification of a negative response element in the human inducible nitric-oxide synthase (hiNOS) promoter: The role of NF-kappa B-repressing factor (NRF) in basal repression of the hiNOS gene
    • Feng X, et al. (2002) Identification of a negative response element in the human inducible nitric-oxide synthase (hiNOS) promoter: The role of NF-kappa B-repressing factor (NRF) in basal repression of the hiNOS gene. Proc Natl Acad Sci USA 99(22):14212-14217.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.22 , pp. 14212-14217
    • Feng, X.1
  • 12
    • 0035830875 scopus 로고    scopus 로고
    • The NF-kappa b repressing factor is involved in basal repression and interleukin (IL)-1-induced activation of IL-8 transcription by binding to a conserved NF-kappa b-flanking sequence element
    • Nourbakhsh M, et al. (2001) The NF-kappa b repressing factor is involved in basal repression and interleukin (IL)-1-induced activation of IL-8 transcription by binding to a conserved NF-kappa b-flanking sequence element. J Biol Chem 276(6):4501-4508.
    • (2001) J Biol Chem , vol.276 , Issue.6 , pp. 4501-4508
    • Nourbakhsh, M.1
  • 13
    • 23844501059 scopus 로고    scopus 로고
    • NF-kappaB-repressing factor inhibits elongation of human immunodeficiency virus type1 transcription by DRB sensitivity-inducing factor
    • Dreikhausen U, Hiebenthal-Millow K, Bartels M, Resch K, Nourbakhsh M (2005) NF-kappaB-repressing factor inhibits elongation of human immunodeficiency virus type1 transcription by DRB sensitivity-inducing factor. Mol Cell Biol 25(17):7473-7483.
    • (2005) Mol Cell Biol , vol.25 , Issue.17 , pp. 7473-7483
    • Dreikhausen, U.1    Hiebenthal-Millow, K.2    Bartels, M.3    Resch, K.4    Nourbakhsh, M.5
  • 14
    • 80455156049 scopus 로고    scopus 로고
    • Mapping of NRF binding motifs of NF-kappaB p65 subunit
    • Reboll MR, et al. (2011) Mapping of NRF binding motifs of NF-kappaB p65 subunit. J Biochem 150(5):553-562.
    • (2011) J Biochem , vol.150 , Issue.5 , pp. 553-562
    • Reboll, M.R.1
  • 15
    • 0031020435 scopus 로고    scopus 로고
    • Inhibition of nuclear factor kappa B by prostaglandin A1: An effect associated with heat shock transcription factor activation
    • Rossi A, Elia G, Santoro MG (1997) Inhibition of nuclear factor kappa B by prostaglandin A1: An effect associated with heat shock transcription factor activation. Proc Natl Acad Sci USA 94(2):746-750.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.2 , pp. 746-750
    • Rossi, A.1    Elia, G.2    Santoro, M.G.3
  • 16
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto RI, Santoro MG (1998) Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection. Nat Biotechnol 16(9):833-838.
    • (1998) Nat Biotechnol , vol.16 , Issue.9 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 17
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase
    • Rossi A, et al. (2000) Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403(6765):103-108.
    • (2000) Nature , vol.403 , Issue.6765 , pp. 103-108
    • Rossi, A.1
  • 18
    • 84883321205 scopus 로고    scopus 로고
    • Transcriptional response to stress in the dynamic chromatin environment of cycling and mitotic cells
    • Vihervaara A, et al. (2013) Transcriptional response to stress in the dynamic chromatin environment of cycling and mitotic cells. Proc Natl Acad Sci USA 110(36):E3388-E3397.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.36 , pp. E3388-E3397
    • Vihervaara, A.1
  • 19
    • 0034127011 scopus 로고    scopus 로고
    • Translation of NRF mRNA is mediated by highly efficient internal ribosome entry
    • Oumard A, Hennecke M, Hauser H, Nourbakhsh M (2000) Translation of NRF mRNA is mediated by highly efficient internal ribosome entry. Mol Cell Biol 20(8):2755-2759.
    • (2000) Mol Cell Biol , vol.20 , Issue.8 , pp. 2755-2759
    • Oumard, A.1    Hennecke, M.2    Hauser, H.3    Nourbakhsh, M.4
  • 20
    • 4444361097 scopus 로고    scopus 로고
    • Nucleolar localization and mobility analysis of the NF-kappaB repressing factor NRF
    • Niedick I, et al. (2004) Nucleolar localization and mobility analysis of the NF-kappaB repressing factor NRF. J Cell Sci 117(Pt 16):3447-3458.
    • (2004) J Cell Sci , vol.117 , pp. 3447-3458
    • Niedick, I.1
  • 23
    • 84892859771 scopus 로고    scopus 로고
    • PAXT-1 promotes XRN2 activity by stabilizing it through a conserved domain
    • Miki TS, Richter H, Rüegger S, Großhans H (2014) PAXT-1 promotes XRN2 activity by stabilizing it through a conserved domain. Mol Cell 53(2):351-360.
    • (2014) Mol Cell , vol.53 , Issue.2 , pp. 351-360
    • Miki, T.S.1    Richter, H.2    Rüegger, S.3    Großhans, H.4
  • 24
    • 84877819839 scopus 로고    scopus 로고
    • XRN 5′→3′ exoribonucleases: Structure, mechanisms and functions
    • Nagarajan VK, Jones CI, Newbury SF, Green PJ (2013) XRN 5′→3′ exoribonucleases: Structure, mechanisms and functions. Biochim Biophys Acta 1829(6-7):590-603.
    • (2013) Biochim Biophys Acta , vol.1829 , Issue.6-7 , pp. 590-603
    • Nagarajan, V.K.1    Jones, C.I.2    Newbury, S.F.3    Green, P.J.4
  • 25
    • 84896527092 scopus 로고    scopus 로고
    • The roles of SSU processome components and surveillance factors in the initial processing of human ribosomal RNA
    • Sloan KE, Bohnsack MT, Schneider C, Watkins NJ (2014) The roles of SSU processome components and surveillance factors in the initial processing of human ribosomal RNA. RNA 20(4):540-550.
    • (2014) RNA , vol.20 , Issue.4 , pp. 540-550
    • Sloan, K.E.1    Bohnsack, M.T.2    Schneider, C.3    Watkins, N.J.4
  • 26
    • 84882641941 scopus 로고    scopus 로고
    • The complexity of human ribosome biogenesis revealed by systematic nucleolar screening of pre-rRNA processing factors
    • Tafforeau L, et al. (2013) The complexity of human ribosome biogenesis revealed by systematic nucleolar screening of pre-rRNA processing factors. Mol Cell 51(4):539-551.
    • (2013) Mol Cell , vol.51 , Issue.4 , pp. 539-551
    • Tafforeau, L.1
  • 27
    • 84874994356 scopus 로고    scopus 로고
    • Both endonucleolytic and exonucleolytic cleavage mediate ITS1 removal during human ribosomal RNA processing
    • Sloan KE, et al. (2013) Both endonucleolytic and exonucleolytic cleavage mediate ITS1 removal during human ribosomal RNA processing. J Cell Biol 200(5):577-588.
    • (2013) J Cell Biol , vol.200 , Issue.5 , pp. 577-588
    • Sloan, K.E.1
  • 28
    • 84877269808 scopus 로고    scopus 로고
    • Gradual processing of the ITS1 from the nucleolus to the cytoplasm during synthesis of the human 18S rRNA
    • Preti M, et al. (2013) Gradual processing of the ITS1 from the nucleolus to the cytoplasm during synthesis of the human 18S rRNA. Nucleic Acids Res 41(8):4709-4723.
    • (2013) Nucleic Acids Res , vol.41 , Issue.8 , pp. 4709-4723
    • Preti, M.1
  • 29
    • 79953141281 scopus 로고    scopus 로고
    • 5′-end surveillance by Xrn2 acts as a shared mechanism for mammalian pre-rRNA maturation and decay
    • Wang M, Pestov DG (2011) 5′-end surveillance by Xrn2 acts as a shared mechanism for mammalian pre-rRNA maturation and decay. Nucleic Acids Res 39(5):1811-1822.
    • (2011) Nucleic Acids Res , vol.39 , Issue.5 , pp. 1811-1822
    • Wang, M.1    Pestov, D.G.2
  • 30
    • 84973459167 scopus 로고    scopus 로고
    • NF-κB-repressing factor phosphorylation regulates transcription elongation via its interactions with 5′→3′ exoribonuclease 2 and negative elongation factor
    • Rother S, et al. (2016) NF-κB-repressing factor phosphorylation regulates transcription elongation via its interactions with 5′→3′ exoribonuclease 2 and negative elongation factor. FASEB J 30(1):174-185.
    • (2016) FASEB J , vol.30 , Issue.1 , pp. 174-185
    • Rother, S.1
  • 32
    • 78650858038 scopus 로고    scopus 로고
    • MiR-301a as an NF-κB activator in pancreatic cancer cells
    • Lu Z, et al. (2011) miR-301a as an NF-κB activator in pancreatic cancer cells. EMBO J 30(1):57-67.
    • (2011) EMBO J , vol.30 , Issue.1 , pp. 57-67
    • Lu, Z.1
  • 33
    • 0033568442 scopus 로고    scopus 로고
    • Induction of ferritin and heat shock proteins by prostaglandin A1 in human monocytes. Evidence for transcriptional and posttranscriptional regulation
    • Elia G, Polla B, Rossi A, Santoro MG (1999) Induction of ferritin and heat shock proteins by prostaglandin A1 in human monocytes. Evidence for transcriptional and posttranscriptional regulation. Eur J Biochem 264(3):736-745.
    • (1999) Eur J Biochem , vol.264 , Issue.3 , pp. 736-745
    • Elia, G.1    Polla, B.2    Rossi, A.3    Santoro, M.G.4
  • 35
    • 0031860393 scopus 로고    scopus 로고
    • Databases on transcriptional regulation: TRANSFAC, TRRD and COMPEL
    • Heinemeyer T, et al. (1998) Databases on transcriptional regulation: TRANSFAC, TRRD and COMPEL. Nucleic Acids Res 26(1):362-367.
    • (1998) Nucleic Acids Res , vol.26 , Issue.1 , pp. 362-367
    • Heinemeyer, T.1
  • 36
    • 77955614928 scopus 로고    scopus 로고
    • Efficient extraction of nucleolar proteins for interactome analyses
    • Chamousset D, Mamane S, Boisvert FM, Trinkle-Mulcahy L (2010) Efficient extraction of nucleolar proteins for interactome analyses. Proteomics 10(16):3045-3050.
    • (2010) Proteomics , vol.10 , Issue.16 , pp. 3045-3050
    • Chamousset, D.1    Mamane, S.2    Boisvert, F.M.3    Trinkle-Mulcahy, L.4
  • 37
    • 84881136339 scopus 로고    scopus 로고
    • Separation of long RNA by agarose-formaldehyde gel electrophoresis
    • Mansour FH, Pestov DG (2013) Separation of long RNA by agarose-formaldehyde gel electrophoresis. Anal Biochem 441(1):18-20.
    • (2013) Anal Biochem , vol.441 , Issue.1 , pp. 18-20
    • Mansour, F.H.1    Pestov, D.G.2
  • 39
    • 84897029324 scopus 로고    scopus 로고
    • Human cell growth regulator Ly-1 antibody reactive homologue accelerates processing of preribosomal RNA
    • Miyazawa N, et al. (2014) Human cell growth regulator Ly-1 antibody reactive homologue accelerates processing of preribosomal RNA. Genes Cells 19(4):273-286.
    • (2014) Genes Cells , vol.19 , Issue.4 , pp. 273-286
    • Miyazawa, N.1


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