메뉴 건너뛰기




Volumn 27, Issue 6, 2008, Pages 827-839

Mutant Huntingtin reduces HSP70 expression through the sequestration of NF-Y transcription factor

Author keywords

Heat shock protein; Huntington's disease; NF Y; Transcription

Indexed keywords

HEAT SHOCK PROTEIN 70; HUNTINGTIN; NUCLEAR FACTOR Y; NUCLEIC ACID BINDING PROTEIN; PROTEIN NFYA; PROTEIN NFYC; UNCLASSIFIED DRUG;

EID: 40949135766     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2008.23     Document Type: Article
Times cited : (100)

References (61)
  • 3
    • 0030842106 scopus 로고    scopus 로고
    • Developmental activation of an episomic hsp70 gene promoter in two-cell mouse embryos by transcription factor Sp1
    • Bevilacqua A, Fiorenza MT, Mangia F (1997) Developmental activation of an episomic hsp70 gene promoter in two-cell mouse embryos by transcription factor Sp1. Nucleic Acids Res 25: 1333-1338
    • (1997) Nucleic Acids Res , vol.25 , pp. 1333-1338
    • Bevilacqua, A.1    Fiorenza, M.T.2    Mangia, F.3
  • 4
    • 0141926491 scopus 로고    scopus 로고
    • Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: A potential mechanism for loss of huntingtin function in Huntington's disease
    • Busch A, Engemann S, Lurz R, Okazawa H, Lehrach H, Wanker EE (2003) Mutant huntingtin promotes the fibrillogenesis of wild-type huntingtin: a potential mechanism for loss of huntingtin function in Huntington's disease. J Biol Chem 278: 41452-41461
    • (2003) J Biol Chem , vol.278 , pp. 41452-41461
    • Busch, A.1    Engemann, S.2    Lurz, R.3    Okazawa, H.4    Lehrach, H.5    Wanker, E.E.6
  • 6
    • 0034283877 scopus 로고    scopus 로고
    • Transcriptional dysregulation in Huntington's disease
    • Cha JH (2000) Transcriptional dysregulation in Huntington's disease. Trends Neurosci 23: 387-392
    • (2000) Trends Neurosci , vol.23 , pp. 387-392
    • Cha, J.H.1
  • 8
    • 0034703863 scopus 로고    scopus 로고
    • Chan HY, Warrick JM, Gray-Board GL, Paulson HL, Bonini NM (2000) Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum Mol Genet 9: 2811-2820
    • Chan HY, Warrick JM, Gray-Board GL, Paulson HL, Bonini NM (2000) Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum Mol Genet 9: 2811-2820
  • 11
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • Doi H, Mitsui K, Kurosawa M, Machida Y, Kuroiwa Y, Nukina N (2004) Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett 571: 171-176
    • (2004) FEBS Lett , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    Machida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 13
    • 36448930958 scopus 로고    scopus 로고
    • Polyglutamine domain modulates the TBP-TFIIB interaction: Implications for its normal function and neurodegeneration
    • Friedman MJ, Shah AG, Fang ZH, Ward EG, Warren ST, Li S, Li XJ (2007) Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration. Nat Neurosci 10: 1519-1528
    • (2007) Nat Neurosci , vol.10 , pp. 1519-1528
    • Friedman, M.J.1    Shah, A.G.2    Fang, Z.H.3    Ward, E.G.4    Warren, S.T.5    Li, S.6    Li, X.J.7
  • 14
    • 27144524290 scopus 로고    scopus 로고
    • Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models
    • Fujimoto M, Takaki E, Hayashi T, Kitaura Y, Tanaka Y, Inouye S, Nakai A (2005) Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. J Biol Chem 280: 34908-34916
    • (2005) J Biol Chem , vol.280 , pp. 34908-34916
    • Fujimoto, M.1    Takaki, E.2    Hayashi, T.3    Kitaura, Y.4    Tanaka, Y.5    Inouye, S.6    Nakai, A.7
  • 15
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • Gidalevitz T, Ben-Zvi A, Ho KH, Brignull HR, Morimoto RI (2006) Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311: 1471-1474
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 16
    • 0023428023 scopus 로고
    • Multiple basal elements of a human hsp70 promoter function differently in human and rodent cell lines
    • Greene JM, Larin Z, Taylor IC, Prentice H, Gwinn KA, Kingston RE (1987) Multiple basal elements of a human hsp70 promoter function differently in human and rodent cell lines. Mol Cell Biol 7: 3646-3655
    • (1987) Mol Cell Biol , vol.7 , pp. 3646-3655
    • Greene, J.M.1    Larin, Z.2    Taylor, I.C.3    Prentice, H.4    Gwinn, K.A.5    Kingston, R.E.6
  • 17
    • 34548259088 scopus 로고    scopus 로고
    • Hsp70 chaperone as a survival factor in cell pathology
    • Guzhova I, Margulis B (2006) Hsp70 chaperone as a survival factor in cell pathology. Int Rev Cytol 254: 101-149
    • (2006) Int Rev Cytol , vol.254 , pp. 101-149
    • Guzhova, I.1    Margulis, B.2
  • 18
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: Interaction partners tell many different stories
    • Harjes P, Wanker EE (2003) The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem Sci 28: 425-433
    • (2003) Trends Biochem Sci , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 19
    • 0032053658 scopus 로고    scopus 로고
    • Characterization of HSE sequences in human Hsp40 gene: Structural and promoter analysis
    • Hata M, Ohtsuka K (1998) Characterization of HSE sequences in human Hsp40 gene: structural and promoter analysis. Biochim Biophys Acta 1397: 43-55
    • (1998) Biochim Biophys Acta , vol.1397 , pp. 43-55
    • Hata, M.1    Ohtsuka, K.2
  • 20
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • Hay DG, Sathasivam K, Tobaben S, Stahl B, Marber M, Mestril R, Mahal A, Smith DL, Woodman B, Bates GP (2004) Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum Mol Genet 13: 1389-1405
    • (2004) Hum Mol Genet , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 22
    • 0035854652 scopus 로고    scopus 로고
    • HSP-CBF is an NF-Y-dependent coactivator of the heat shock promoters CCAAT boxes
    • Imbriano C, Bolognese F, Gurtner A, Piaggio G, Mantovani R (2001) HSP-CBF is an NF-Y-dependent coactivator of the heat shock promoters CCAAT boxes. J Biol Chem 276: 26332-26339
    • (2001) J Biol Chem , vol.276 , pp. 26332-26339
    • Imbriano, C.1    Bolognese, F.2    Gurtner, A.3    Piaggio, G.4    Mantovani, R.5
  • 23
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • Jana NR, Tanaka M, Wang G, Nukina N (2000) Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum Mol Genet 9: 2009-2018
    • (2000) Hum Mol Genet , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 24
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P, Benzer S (2000) Genetic suppression of polyglutamine toxicity in Drosophila. Science 287: 1837-1840
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 26
    • 34547839797 scopus 로고    scopus 로고
    • Kuhn A, Goldstein DR, Hodges A, Strand AD, Sengstag T, Kooperberg C, Becanovic K, Pouladi MA, Sathasivam K, Cha JH, Hannan AJ, Hayden MR, Leavitt BR, Dunnett SB, Ferrante RJ, Albin R, Shelbourne P, Delorenzi M, Augood SJ, Faull RL et al (2007) Mutant huntingtin's effects on striatal gene expression in mice recapitulate changes observed in human Huntington's disease brain and do not differ with mutant huntingtin length or wild-type huntingtin dosage. Hum Mol Genet 16: 1845-1861
    • Kuhn A, Goldstein DR, Hodges A, Strand AD, Sengstag T, Kooperberg C, Becanovic K, Pouladi MA, Sathasivam K, Cha JH, Hannan AJ, Hayden MR, Leavitt BR, Dunnett SB, Ferrante RJ, Albin R, Shelbourne P, Delorenzi M, Augood SJ, Faull RL et al (2007) Mutant huntingtin's effects on striatal gene expression in mice recapitulate changes observed in human Huntington's disease brain and do not differ with mutant huntingtin length or wild-type huntingtin dosage. Hum Mol Genet 16: 1845-1861
  • 27
    • 8844220536 scopus 로고    scopus 로고
    • Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series
    • Landles C, Bates GP (2004) Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series. EMBO Rep 5: 958-963
    • (2004) EMBO Rep , vol.5 , pp. 958-963
    • Landles, C.1    Bates, G.P.2
  • 28
    • 0032476596 scopus 로고    scopus 로고
    • Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo
    • Li Q, Herrler M, Landsberger N, Kaludov N, Ogryzko VV, Nakatani Y, Wolffe AP (1998) Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo. EMBO J 17: 6300-6315
    • (1998) EMBO J , vol.17 , pp. 6300-6315
    • Li, Q.1    Herrler, M.2    Landsberger, N.3    Kaludov, N.4    Ogryzko, V.V.5    Nakatani, Y.6    Wolffe, A.P.7
  • 29
    • 0036173896 scopus 로고    scopus 로고
    • Interaction of Huntington disease protein with transcriptional activator Sp1
    • Li SH, Cheng AL, Zhou H, Lam S, Rao M, Li H, Li XJ (2002) Interaction of Huntington disease protein with transcriptional activator Sp1. Mol Cell Biol 22: 1277-1287
    • (2002) Mol Cell Biol , vol.22 , pp. 1277-1287
    • Li, S.H.1    Cheng, A.L.2    Zhou, H.3    Lam, S.4    Rao, M.5    Li, H.6    Li, X.J.7
  • 30
    • 1242338856 scopus 로고    scopus 로고
    • Huntingtin-protein interactions and the pathogenesis of Huntington's disease
    • Li SH, Li XJ (2004) Huntingtin-protein interactions and the pathogenesis of Huntington's disease. Trends Genet 20: 146-154
    • (2004) Trends Genet , vol.20 , pp. 146-154
    • Li, S.H.1    Li, X.J.2
  • 32
    • 0032078929 scopus 로고    scopus 로고
    • Role of the CCAAT-binding protein CBF/NF-Y in transcription
    • Maity SN, de Crombrugghe B (1998) Role of the CCAAT-binding protein CBF/NF-Y in transcription. Trends Biochem Sci 23: 174-178
    • (1998) Trends Biochem Sci , vol.23 , pp. 174-178
    • Maity, S.N.1    de Crombrugghe, B.2
  • 34
    • 0032851812 scopus 로고    scopus 로고
    • The molecular biology of the CCAAT-binding factor NF-Y
    • Mantovani R (1999) The molecular biology of the CCAAT-binding factor NF-Y. Gene 239: 15-27
    • (1999) Gene , vol.239 , pp. 15-27
    • Mantovani, R.1
  • 35
    • 33645214602 scopus 로고    scopus 로고
    • Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells
    • Matsumoto G, Kim S, Morimoto RI (2006) Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells. J Biol Chem 281: 4477-4485
    • (2006) J Biol Chem , vol.281 , pp. 4477-4485
    • Matsumoto, G.1    Kim, S.2    Morimoto, R.I.3
  • 36
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62: 670-684
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 37
    • 0038269098 scopus 로고    scopus 로고
    • Polyglutamine expansion induces a protein-damaging stress connecting heat shock protein 70 to the JNK pathway
    • Merienne K, Helmlinger D, Perkin GR, Devys D, Trottier Y (2003) Polyglutamine expansion induces a protein-damaging stress connecting heat shock protein 70 to the JNK pathway. J Biol Chem 278: 16957-16967
    • (2003) J Biol Chem , vol.278 , pp. 16957-16967
    • Merienne, K.1    Helmlinger, D.2    Perkin, G.R.3    Devys, D.4    Trottier, Y.5
  • 38
    • 0024414620 scopus 로고
    • Transcription factor Sp1 binds to and activates a human hsp70 gene promoter
    • Morgan WD (1989) Transcription factor Sp1 binds to and activates a human hsp70 gene promoter. Mol Cell Biol 9: 4099-4104
    • (1989) Mol Cell Biol , vol.9 , pp. 4099-4104
    • Morgan, W.D.1
  • 39
    • 0023132206 scopus 로고
    • Two transcriptional activators, CCAAT-box-binding transcription factor and heat shock transcription factor, interact with a human hsp70 gene promoter
    • Morgan WD, Williams GT, Morimoto RI, Greene J, Kingston RE, Tjian R (1987) Two transcriptional activators, CCAAT-box-binding transcription factor and heat shock transcription factor, interact with a human hsp70 gene promoter. Mol Cell Biol 7: 1129-1138
    • (1987) Mol Cell Biol , vol.7 , pp. 1129-1138
    • Morgan, W.D.1    Williams, G.T.2    Morimoto, R.I.3    Greene, J.4    Kingston, R.E.5    Tjian, R.6
  • 40
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells
    • Mosser DD, Theodorakis NG, Morimoto RI (1988) Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells. Mol Cell Biol 8: 4736-4744
    • (1988) Mol Cell Biol , vol.8 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 42
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins
    • Nollen EA, Morimoto RI (2002) Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. J Cell Sci 115: 2809-2816
    • (2002) J Cell Sci , vol.115 , pp. 2809-2816
    • Nollen, E.A.1    Morimoto, R.I.2
  • 44
    • 0742287915 scopus 로고    scopus 로고
    • CRE-mediated transcription is increased in Huntington's disease transgenic mice
    • Obrietan K, Hoyt KR (2004) CRE-mediated transcription is increased in Huntington's disease transgenic mice. J Neurosci 24: 791-796
    • (2004) J Neurosci , vol.24 , pp. 791-796
    • Obrietan, K.1    Hoyt, K.R.2
  • 47
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • Sakahira H, Breuer P, Hayer-Hartl MK, Hartl FU (2002) Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc Natl Acad Sci USA 99 (Suppl 4): 16412-16418
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.SUPPL. 4 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 51
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars KL, Rubinsztein DC (2003) Transcriptional abnormalities in Huntington disease. Trends Genet 19: 233-238
    • (2003) Trends Genet , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 52
    • 0035897405 scopus 로고    scopus 로고
    • Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression
    • Suhr ST, Senut MC, Whitelegge JP, Faull KF, Cuizon DB, Gage FH (2001) Identities of sequestered proteins in aggregates from cells with induced polyglutamine expression. J Cell Biol 153: 283-294
    • (2001) J Cell Biol , vol.153 , pp. 283-294
    • Suhr, S.T.1    Senut, M.C.2    Whitelegge, J.P.3    Faull, K.F.4    Cuizon, D.B.5    Gage, F.H.6
  • 54
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72: 971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 56
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker JL, Zareie MH, Fong H, Sarikaya M, Muchowski PJ (2004) Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat Struct Mol Biol 11: 1215-1222
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 57
    • 0033867992 scopus 로고    scopus 로고
    • Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B
    • Wang G, Sawai N, Kotliarova S, Kanazawa I, Nukina N (2000) Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Hum Mol Genet 9: 1795-1803
    • (2000) Hum Mol Genet , vol.9 , pp. 1795-1803
    • Wang, G.1    Sawai, N.2    Kotliarova, S.3    Kanazawa, I.4    Nukina, N.5
  • 58
    • 0012111663 scopus 로고
    • Human HSP70 promoter contains at least two distinct regulatory domains
    • Wu BJ, Kingston RE, Morimoto RI (1986) Human HSP70 promoter contains at least two distinct regulatory domains. Proc Natl Acad Sci USA 83: 629-633
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 629-633
    • Wu, B.J.1    Kingston, R.E.2    Morimoto, R.I.3
  • 59
    • 33745217610 scopus 로고    scopus 로고
    • Lgl mediates apical domain disassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity
    • Yamanaka T, Horikoshi Y, Izumi N, Suzuki A, Mizuno K, Ohno S (2006) Lgl mediates apical domain disassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity. J Cell Sci 119: 2107-2118
    • (2006) J Cell Sci , vol.119 , pp. 2107-2118
    • Yamanaka, T.1    Horikoshi, Y.2    Izumi, N.3    Suzuki, A.4    Mizuno, K.5    Ohno, S.6
  • 60
    • 0037090927 scopus 로고    scopus 로고
    • Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice
    • Yu ZX, Li SH, Nguyen HP, Li XJ (2002) Huntingtin inclusions do not deplete polyglutamine-containing transcription factors in HD mice. Hum Mol Genet 11: 905-914
    • (2002) Hum Mol Genet , vol.11 , pp. 905-914
    • Yu, Z.X.1    Li, S.H.2    Nguyen, H.P.3    Li, X.J.4
  • 61
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • Zhou H, Li SH, Li XJ (2001) Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J Biol Chem 276: 48417-48424
    • (2001) J Biol Chem , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.H.2    Li, X.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.