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Volumn 1, Issue 1, 2012, Pages 33-45

Polyglutamine expanded huntingtin dramatically alters the genome-wide binding of HSF1

Author keywords

cDNA microarrays; chromatin immunoprecipitation; deep sequencing; heat shock transcription factor; heat shock response; Huntington disease

Indexed keywords

GUANOSINE TRIPHOSPHATASE; HEAT SHOCK TRANSCRIPTION FACTOR 1; HUNTINGTIN; POLYGLUTAMINE; DNA BINDING PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR; HTT PROTEIN, HUMAN; NERVE PROTEIN; PEPTIDE; TRANSCRIPTION FACTOR;

EID: 84880757782     PISSN: 18796397     EISSN: 18796400     Source Type: Journal    
DOI: 10.3233/JHD-2012-120020     Document Type: Article
Times cited : (36)

References (60)
  • 1
    • 0027480960 scopus 로고
    • Anovel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • Anovel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell. 1993;72(6):971-83.
    • (1993) Cell , vol.72 , Issue.6 , pp. 971-983
  • 2
    • 0142139321 scopus 로고    scopus 로고
    • Huntington's disease
    • MacDonald ME, et al. Huntington's disease. Neuromolecular Med. 2003;4(1-2):7-20.
    • (2003) Neuromolecular Med , vol.4 , Issue.1-2 , pp. 7-20
    • Macdonald, M.E.1
  • 3
    • 77955844171 scopus 로고    scopus 로고
    • Chaperone networks: Tipping the balance in protein folding diseases
    • Voisine C, Pedersen JS, Morimoto RI. Chaperone networks: Tipping the balance in protein folding diseases. Neurobiol Dis. 2010;40(1):12-20.
    • (2010) Neurobiol Dis , vol.40 , Issue.1 , pp. 12-20
    • Voisine, C.1    Pedersen, J.S.2    Morimoto, R.I.3
  • 4
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N, et al. Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J Biol Chem. 2008;283(38):26188-97.
    • (2008) J Biol Chem , vol.283 , Issue.38 , pp. 26188-26197
    • Fujikake, N.1
  • 5
    • 12944335007 scopus 로고    scopus 로고
    • Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutaminemediated aggregation
    • Wang J, et al. Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutaminemediated aggregation. BMC Neurosci. 2005;6:1.
    • (2005) BMC Neurosci , vol.6 , pp. 1
    • Wang, J.1
  • 8
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • DOI 10.1074/jbc.R500010200
    • Westerheide SD, Morimoto RI. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem. 2005;280(39):33097-100. (Pubitemid 41397104)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.39 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 9
    • 36849044616 scopus 로고    scopus 로고
    • Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response
    • DOI 10.1007/s00109-007-0251-9, Special Issue (Ed. G. Semenza): Hypoxia and Human Disease
    • Zhang YQ, Sarge KD. Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response. J Mol Med (Berl). 2007;85(12):1421-8. (Pubitemid 350234097)
    • (2007) Journal of Molecular Medicine , vol.85 , Issue.12 , pp. 1421-1428
    • Zhang, Y.-Q.1    Sarge, K.D.2
  • 12
    • 82455210670 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
    • Neef DW, Jaeger AM, Thiele DJ. Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases. Nat Rev Drug Discov. 2011;10(12):930-44.
    • (2011) Nat Rev Drug Discov , vol.10 , Issue.12 , pp. 930-944
    • Neef, D.W.1    Jaeger, A.M.2    Thiele, D.J.3
  • 13
    • 75749136948 scopus 로고    scopus 로고
    • Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease
    • Neef DW, Turski ML, Thiele DJ. Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol. 2010;8(1):e1000291.
    • (2010) PLoS Biol , vol.8 , Issue.1
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 14
    • 84934443868 scopus 로고    scopus 로고
    • Heat shock factor 1 as a coordinator of stress and developmental pathways
    • Anckar J, Sistonen L. Heat shock factor 1 as a coordinator of stress and developmental pathways. Adv Exp Med Biol. 2007;594:78-88.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 78-88
    • Anckar, J.1    Sistonen, L.2
  • 15
    • 2942598422 scopus 로고    scopus 로고
    • Genome-wide analysis of the biology of stress responses through heat shock transcription factor
    • Hahn JS, et al. Genome-wide analysis of the biology of stress responses through heat shock transcription factor. Mol Cell Biol. 2004;24(12):5249-56.
    • (2004) Mol Cell Biol , vol.24 , Issue.12 , pp. 5249-5256
    • Hahn, J.S.1
  • 16
    • 28844475890 scopus 로고    scopus 로고
    • Genomic analysis of heat-shock factor targets in Drosophila
    • Birch-Machin I, et al. Genomic analysis of heat-shock factor targets in Drosophila. Genome Biol. 2005;6(7):R63.
    • (2005) Genome Biol , vol.6 , Issue.7
    • Birch-Machin, I.1
  • 17
    • 33751092252 scopus 로고    scopus 로고
    • Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival
    • DOI 10.1039/b606129j
    • Page TJ, et al. Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival. Mol Biosyst. 2006;2(12):627-39. (Pubitemid 44772306)
    • (2006) Molecular BioSystems , vol.2 , Issue.12 , pp. 627-639
    • Page, T.J.1    Sikder, D.2    Yang, L.3    Pluta, L.4    Wolfinger, R.D.5    Kodadek, T.6    Thomas, R.S.7
  • 18
    • 34547420555 scopus 로고    scopus 로고
    • Demyelination, astrogliosis, and accumulation of ubiquitinated proteins, hallmarks of CNS disease in hsf1-deficient mice
    • DOI 10.1523/JNEUROSCI.0006-07.2007
    • Homma S, et al. Demyelination, astrogliosis, and accumulation of ubiquitinated proteins, hallmarks of CNS disease in hsf1-deficient mice. J Neurosci. 2007;27(30):7974-86. (Pubitemid 47173325)
    • (2007) Journal of Neuroscience , vol.27 , Issue.30 , pp. 7974-7986
    • Homma, S.1    Jin, X.2    Wang, G.3    Tu, N.4    Min, J.5    Yanasak, N.6    Mivechi, N.F.7
  • 19
    • 34548658230 scopus 로고    scopus 로고
    • Heat Shock Factor 1 Is a Powerful Multifaceted Modifier of Carcinogenesis
    • DOI 10.1016/j.cell.2007.07.020, PII S0092867407009579
    • Dai C, et al. Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell. 2007;130(6):1005-18. (Pubitemid 47410269)
    • (2007) Cell , vol.130 , Issue.6 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 20
    • 0034703869 scopus 로고    scopus 로고
    • Dominant phenotypes produced by the HD mutation in STHdh(Q111) striatal cells
    • Trettel F, et al. Dominant phenotypes produced by the HD mutation in STHdh(Q111) striatal cells. Hum Mol Genet. 2000;9(19):2799-809.
    • (2000) Hum Mol Genet , vol.9 , Issue.19 , pp. 2799-2809
    • Trettel, F.1
  • 21
    • 79961013560 scopus 로고    scopus 로고
    • Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease
    • Labbadia J, et al. Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease. J Clin Invest. 2011;121(8): 3306-19.
    • (2011) J Clin Invest , vol.121 , Issue.8 , pp. 3306-3319
    • Labbadia, J.1
  • 22
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • DOI 10.1091/mbc.E03-10-0738
    • Trinklein ND, et al. The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol Biol Cell. 2004;15(3):1254-61. (Pubitemid 38316232)
    • (2004) Molecular biology of the 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
  • 23
    • 83155173181 scopus 로고    scopus 로고
    • Neurodegenerative processes in Huntington's disease
    • Bano D, et al. Neurodegenerative processes in Huntington's disease. Cell Death Dis. 2011;2:e228.
    • (2011) Cell Death Dis , vol.2
    • Bano, D.1
  • 24
    • 79955955066 scopus 로고    scopus 로고
    • Proteasomal dysfunction in aging and Huntington disease
    • Li XJ, Li S. Proteasomal dysfunction in aging and Huntington disease. Neurobiol Dis. 2011;43(1):4-8.
    • (2011) Neurobiol Dis , vol.43 , Issue.1 , pp. 4-8
    • Li, X.J.1    Li, S.2
  • 26
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang da W, Sherman BT, Lempicki RA. Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat Protoc. 2009;4(1):44-57.
    • (2009) Nat Protoc , vol.4 , Issue.1 , pp. 44-57
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 27
    • 58549112996 scopus 로고    scopus 로고
    • Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists
    • Huang da W, Sherman BT, Lempicki RA. Bioinformatics enrichment tools: Paths toward the comprehensive functional analysis of large gene lists. Nucleic Acids Res. 2009;37(1):1-13.
    • (2009) Nucleic Acids Res , vol.37 , Issue.1 , pp. 1-13
    • Huang Da, W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 29
    • 34548399406 scopus 로고    scopus 로고
    • Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism
    • Lee JM, et al. Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism. PLoS Genet. 2007;3(8):e135.
    • (2007) PLoS Genet , vol.3 , Issue.8
    • Lee, J.M.1
  • 30
    • 0035862896 scopus 로고    scopus 로고
    • Neurological abnormalities in a knock-in mouse model of Huntington's disease
    • Lin CH, et al. Neurological abnormalities in a knock-in mouse model of Huntington's disease. Hum Mol Genet. 2001;10(2):137-44.
    • (2001) Hum Mol Genet , vol.10 , Issue.2 , pp. 137-144
    • Lin, C.H.1
  • 32
    • 66149110042 scopus 로고    scopus 로고
    • A large number of protein expression changes occur early in life and precede phenotype onset in a mouse model for huntington disease
    • Zabel C, et al. A large number of protein expression changes occur early in life and precede phenotype onset in a mouse model for huntington disease. Mol Cell Proteomics. 2009; 8(4):720-34.
    • (2009) Mol Cell Proteomics , vol.8 , Issue.4 , pp. 720-734
    • Zabel, C.1
  • 33
    • 34249715853 scopus 로고    scopus 로고
    • Huntingtin interacting proteins are genetic modifiers of neurodegeneration
    • Kaltenbach LS, et al. Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genet. 2007;3(5):e82.
    • (2007) PLoS Genet , vol.3 , Issue.5
    • Kaltenbach, L.S.1
  • 34
    • 79955456732 scopus 로고    scopus 로고
    • Mutant huntingtin causes defective actin remodeling during stress: Defining a new role for transglutaminase 2 in neurodegenerative disease
    • Munsie L, et al. Mutant huntingtin causes defective actin remodeling during stress: Defining a new role for transglutaminase 2 in neurodegenerative disease. Hum Mol Genet. 2011;20(10):1937-51.
    • (2011) Hum Mol Genet , vol.20 , Issue.10 , pp. 1937-1951
    • Munsie, L.1
  • 38
    • 0036500862 scopus 로고    scopus 로고
    • Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with β-tubulin: Relevance to Huntington's disease
    • Hoffner G, Kahlem P, Djian P. Perinuclear localization of huntingtin as a consequence of its binding to microtubules through an interaction with beta-tubulin: Relevance to Huntington's disease. J Cell Sci. 2002;115(Pt 5):941-8. (Pubitemid 34257379)
    • (2002) Journal of Cell Science , vol.115 , Issue.5 , pp. 941-948
    • Hoffner, G.1    Kahlem, P.2    Djian, P.3
  • 39
    • 0030819255 scopus 로고    scopus 로고
    • Huntington's disease gene product, huntingtin, associates with microtubules in vitro
    • DOI 10.1016/S0169-328X(97)00205-2, PII S0169328X97002052
    • Tukamoto T, et al. Huntington's disease gene product, huntingtin, associates with microtubules in vitro. Brain Res Mol Brain Res. 1997;51(1-2):8-14. (Pubitemid 27504026)
    • (1997) Molecular Brain Research , vol.51 , Issue.1-2 , pp. 8-14
    • Tukamoto, T.1    Nukina, N.2    Ide, K.3    Kanazawa, I.4
  • 41
    • 78650347671 scopus 로고    scopus 로고
    • Neuronal LRP1 knockout in adult mice leads to impaired brain lipid metabolism and progressive, age-dependent synapse loss and neurodegeneration
    • Liu Q, et al. Neuronal LRP1 knockout in adult mice leads to impaired brain lipid metabolism and progressive, age-dependent synapse loss and neurodegeneration. J neurosci. 2010;30(50):17068-17078.
    • (2010) J Neurosci , vol.30 , Issue.50 , pp. 17068-17078
    • Liu, Q.1
  • 42
    • 71949120013 scopus 로고    scopus 로고
    • Mutant huntingtin impairs vesicle formation from recycling endosomes by interfering with Rab11 activity
    • Li X, et al. Mutant huntingtin impairs vesicle formation from recycling endosomes by interfering with Rab11 activity. Mol Cell Biol. 2009;29(22):6106-16.
    • (2009) Mol Cell Biol , vol.29 , Issue.22 , pp. 6106-6116
    • Li, X.1
  • 43
    • 79952033383 scopus 로고    scopus 로고
    • In vivo cell-autonomous transcriptional abnormalities revealed in mice expressing mutant huntingtin in striatal but not cortical neurons
    • Thomas E, et al. In vivo cell-autonomous transcriptional abnormalities revealed in mice expressing mutant huntingtin in striatal but not cortical neurons. Hum Mol Genet. 2011;20(6):1049-60.
    • (2011) Hum Mol Genet , vol.20 , Issue.6 , pp. 1049-1060
    • Thomas, E.1
  • 44
    • 67650061723 scopus 로고    scopus 로고
    • Impaired PGC-1alpha function in muscle in Huntington's disease
    • Chaturvedi RK, et al. Impaired PGC-1alpha function in muscle in Huntington's disease. Hum Mol Genet. 2009; 18(16):3048-65.
    • (2009) Hum Mol Genet , vol.18 , Issue.16 , pp. 3048-3065
    • Chaturvedi, R.K.1
  • 45
    • 70349111436 scopus 로고    scopus 로고
    • Emerging roles of peroxisome proliferator-activated receptor-beta/delta in inflammation
    • Bishop-Bailey D, Bystrom J. Emerging roles of peroxisome proliferator-activated receptor-beta/delta in inflammation. Pharmacol Ther. 2009;124(2):141-50.
    • (2009) Pharmacol Ther , vol.124 , Issue.2 , pp. 141-150
    • Bishop-Bailey, D.1    Bystrom, J.2
  • 46
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • DOI 10.1126/science.292.5521.1552
    • Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 2001;292(5521):1552-5. (Pubitemid 32493425)
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 47
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • DOI 10.1016/j.molcel.2004.12.021, PII S1097276505010087
    • Bennett EJ, et al. Global impairment of the ubiquitinproteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell. 2005; 17(3):351-65. (Pubitemid 40193307)
    • (2005) Molecular Cell , vol.17 , Issue.3 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 50
    • 0041330609 scopus 로고    scopus 로고
    • Impaired degradation of PKCα by proteasome in a cellular model of Huntington's disease
    • DOI 10.1097/00001756-200308060-00006
    • Zemskov EA, Nukina N, Impaired degradation of PKCalpha by proteasome in a cellular model of Huntington's disease. Neuroreport. 2003;14(11):1435-8. (Pubitemid 37083123)
    • (2003) NeuroReport , vol.14 , Issue.11 , pp. 1435-1438
    • Zemskov, E.A.1    Nukina, N.2
  • 51
    • 72449141635 scopus 로고    scopus 로고
    • Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
    • Fuchs M, et al. Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction. Biochem J. 2010;425(1):245-55.
    • (2010) Biochem J , vol.425 , Issue.1 , pp. 245-255
    • Fuchs, M.1
  • 52
    • 12344280017 scopus 로고    scopus 로고
    • Summaries of Affymetrix GeneChip probe level data
    • Irizarry RA, et al. Summaries of Affymetrix GeneChip probe level data. Nucleic Acids Res. 2003;31(4):e15.
    • (2003) Nucleic Acids Res , vol.31 , Issue.4
    • Irizarry, R.A.1
  • 53
    • 4544341015 scopus 로고    scopus 로고
    • Linear models and empirical bayes methods for assessing differential expression in microarray experiments
    • Smyth GK, Linear models and empirical bayes methods for assessing differential expression in microarray experiments. Stat Appl Genet Mol Biol. 2004;3:Article3.
    • (2004) Stat Appl Genet Mol Biol , vol.3
    • Smyth, G.K.1
  • 54
    • 1542338426 scopus 로고    scopus 로고
    • Transcriptional regulation and binding of heat shock factor 1 and heat shock factor 2 to 32 human heat shock genes during thermal stress and differentiation
    • DOI 10.1379/1466-1268(2004)009 <0021:TRABOH>2.0.CO;2
    • Trinklein ND, et al. Transcriptional regulation and binding of heat shock factor 1 and heat shock factor 2 to 32 human heat shock genes during thermal stress and differentiation. Cell Stress Chaperones. 2004;9(1):21-8. (Pubitemid 38429072)
    • (2004) Cell Stress and Chaperones , vol.9 , Issue.1 , pp. 21-28
    • Trinklein, N.D.1    Chen, W.C.2    Kingston, R.E.3    Myers, R.M.4
  • 55
    • 77954586080 scopus 로고    scopus 로고
    • A quantitative model of transcriptional regulation reveals the influence of binding location on expression
    • MacIsaac KD, et al. A quantitative model of transcriptional regulation reveals the influence of binding location on expression. PLoS Comput Biol. 2010;6(4):e1000773.
    • (2010) PLoS Comput Biol , vol.6 , Issue.4
    • Macisaac, K.D.1
  • 56
    • 53849146020 scopus 로고    scopus 로고
    • Model-based analysis of ChIP-Seq (MACS)
    • Zhang Y, et al. Model-based analysis of ChIP-Seq (MACS). Genome Biol. 2008;9(9):R137.
    • (2008) Genome Biol , vol.9 , Issue.9
    • Zhang, Y.1
  • 57
    • 58149178565 scopus 로고    scopus 로고
    • The UCSC genome browser database: Update 2009
    • Kuhn RM, et al. The UCSC Genome Browser Database: Update 2009. Nucleic Acids Res. 2009;37(Database issue): D755-61.
    • (2009) Nucleic Acids Res , vol.37 , Issue.DATABASE ISSUE
    • Kuhn, R.M.1
  • 58
    • 32544434809 scopus 로고    scopus 로고
    • A hypothesis-based approach for identifying the binding specificity of regulatory proteins from chromatin immunoprecipitation data
    • Macisaac KD, et al. A hypothesis-based approach for identifying the binding specificity of regulatory proteins from chromatin immunoprecipitation data. Bioinformatics. 2006; 22(4):423-9.
    • (2006) Bioinformatics , vol.22 , Issue.4 , pp. 423-429
    • Macisaac, K.D.1
  • 60
    • 78651310799 scopus 로고    scopus 로고
    • Database resources of the National Center for Biotechnology Information
    • Sayers EW, et al. Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 2010;39(Database issue):D38-51.
    • (2010) Nucleic Acids Res , vol.39 , Issue.DATABASE ISSUE
    • Sayers, E.W.1


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