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Volumn 396, Issue 3, 2010, Pages 742-747

Altered microRNAs in STHdhQ111/HdhQ111 cells: miR-146a targets TBP

Author keywords

MicroRNA 146a; STHdhQ111 HdhQ111 cells; Tata Binding Protein

Indexed keywords

MICRORNA; MICRORNA 146A; TATA BINDING PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UNCLASSIFIED DRUG;

EID: 77953025795     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.05.007     Document Type: Article
Times cited : (61)

References (39)
  • 1
    • 41549110185 scopus 로고    scopus 로고
    • Control of protein synthesis and mRNA degradation by microRNAs
    • Liu J. Control of protein synthesis and mRNA degradation by microRNAs. Curr. Opin. Cell Biol. 20 (2008) 214-221
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 214-221
    • Liu, J.1
  • 2
    • 11844278458 scopus 로고    scopus 로고
    • Conserved seed pairing, often flanked by adenosines, indicates that thousands of human genes are microRNA targets
    • Lewis B.P., Burge C.B., and Bartel D.P. Conserved seed pairing, often flanked by adenosines, indicates that thousands of human genes are microRNA targets. Cell 120 (2005) 15-20
    • (2005) Cell , vol.120 , pp. 15-20
    • Lewis, B.P.1    Burge, C.B.2    Bartel, D.P.3
  • 3
    • 28044439909 scopus 로고    scopus 로고
    • A cAMP-response element binding protein-induced microRNA regulates neuronal morphogenesis
    • Vo N., Klein M.E., Varlamova O., et al. A cAMP-response element binding protein-induced microRNA regulates neuronal morphogenesis. Proc. Natl. Acad. Sci. USA 102 (2005) 16426-16431
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16426-16431
    • Vo, N.1    Klein, M.E.2    Varlamova, O.3
  • 4
    • 35748961986 scopus 로고    scopus 로고
    • p53 enters the microRNA world
    • Hermeking H. p53 enters the microRNA world. Cancer Cell 12 (2007) 414-418
    • (2007) Cancer Cell , vol.12 , pp. 414-418
    • Hermeking, H.1
  • 5
    • 77349120755 scopus 로고    scopus 로고
    • PhenomiR: a knowledgebase for microRNA expression in diseases and biological processes
    • (Epub ahead of print)
    • Ruepp A., Kowarsch A., Schmidl D., et al. PhenomiR: a knowledgebase for microRNA expression in diseases and biological processes. Genome Biol. 11 (2010) R6 (Epub ahead of print)
    • (2010) Genome Biol. , vol.11
    • Ruepp, A.1    Kowarsch, A.2    Schmidl, D.3
  • 6
    • 58149179989 scopus 로고    scopus 로고
    • MiR2Disease: a manually curated database for microRNA deregulation in human disease
    • Jiang Q., Wang Y., Hao Y., et al. MiR2Disease: a manually curated database for microRNA deregulation in human disease. Nucl. Acid Res. 37 (2009) D98-D104
    • (2009) Nucl. Acid Res. , vol.37
    • Jiang, Q.1    Wang, Y.2    Hao, Y.3
  • 7
    • 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. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72 (1993) 971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 8
    • 44449131447 scopus 로고    scopus 로고
    • Huntington's disease: from pathology and genetics to potential therapies
    • Imarisio S., Carmichael J.V., Korolchuk V., et al. Huntington's disease: from pathology and genetics to potential therapies. Biochem. J. 412 (2008) 191-209
    • (2008) Biochem. J. , vol.412 , pp. 191-209
    • Imarisio, S.1    Carmichael, J.V.2    Korolchuk, V.3
  • 9
    • 35348877164 scopus 로고    scopus 로고
    • Transcriptional signatures in Huntington's disease
    • Cha J.H. Transcriptional signatures in Huntington's disease. Prog. Neurobiol. 83 (2007) 228-248
    • (2007) Prog. Neurobiol. , vol.83 , pp. 228-248
    • Cha, J.H.1
  • 10
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars K.L., and Rubinsztein D.C. Transcriptional abnormalities in Huntington disease. Trends Genet. 19 (2003) 233-238
    • (2003) Trends Genet. , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 11
    • 0041353535 scopus 로고    scopus 로고
    • Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE controlled neuronal genes
    • Zucatto C., Tartari M., Crotti A., et al. Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE controlled neuronal genes. Nat. Genet. 35 (2003) 76-83
    • (2003) Nat. Genet. , vol.35 , pp. 76-83
    • Zucatto, C.1    Tartari, M.2    Crotti, A.3
  • 12
    • 54849422301 scopus 로고    scopus 로고
    • Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner
    • Benn C.L., Sun T., Sadri-Vakili G., et al. Huntingtin modulates transcription, occupies gene promoters in vivo, and binds directly to DNA in a polyglutamine-dependent manner. J. Neurosci. 28 (2008) 10720-10733
    • (2008) J. Neurosci. , vol.28 , pp. 10720-10733
    • Benn, C.L.1    Sun, T.2    Sadri-Vakili, G.3
  • 13
    • 39649092720 scopus 로고    scopus 로고
    • A microRNA-based gene dysregulation pathway in Huntington's disease
    • Johnson R., Zuccato C., Belyaev N.D., et al. A microRNA-based gene dysregulation pathway in Huntington's disease. Neurobiol. Dis. 29 (2008) 438-445
    • (2008) Neurobiol. Dis. , vol.29 , pp. 438-445
    • Johnson, R.1    Zuccato, C.2    Belyaev, N.D.3
  • 14
    • 58149375393 scopus 로고    scopus 로고
    • The bifunctional microRNA miR-9/miR-9* regulates REST and CoREST and is downregulated in Huntington's disease
    • Packer A.N., Xing Y., Harper S.Q., et al. The bifunctional microRNA miR-9/miR-9* regulates REST and CoREST and is downregulated in Huntington's disease. J. Neurosci. 28 (2008) 14341-14346
    • (2008) J. Neurosci. , vol.28 , pp. 14341-14346
    • Packer, A.N.1    Xing, Y.2    Harper, S.Q.3
  • 15
    • 77952584652 scopus 로고    scopus 로고
    • P. Lau, B. de Strooper, Dysregulated microRNAs in neurodegenerative disorders, Semin. Cell Dev. Biol. 2010 (Epub ahead of print).
    • P. Lau, B. de Strooper, Dysregulated microRNAs in neurodegenerative disorders, Semin. Cell Dev. Biol. 2010 (Epub ahead of print).
  • 16
    • 24344459888 scopus 로고    scopus 로고
    • Possible role for p53 in Huntington's disease
    • Burton A. Possible role for p53 in Huntington's disease. Lancet Neurol. 4 9 (2005) 528-529
    • (2005) Lancet Neurol. , vol.4 , Issue.9 , pp. 528-529
    • Burton, A.1
  • 17
    • 49449091708 scopus 로고    scopus 로고
    • Huntington's disease protein contributes to RNA-mediated gene silencing through association with Argonaute and P bodies
    • Savas J.N., Makusky A., Ottosen S., et al. Huntington's disease protein contributes to RNA-mediated gene silencing through association with Argonaute and P bodies. Proc. Natl. Acad. Sci. USA 105 (2008) 10820-10825
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10820-10825
    • Savas, J.N.1    Makusky, A.2    Ottosen, S.3
  • 18
    • 67749143728 scopus 로고    scopus 로고
    • Modulation of microRNA processing by p53
    • Suzuki H.I., Yamagata K., Sugimoto K., et al. Modulation of microRNA processing by p53. Nature 460 (2009) 529-533
    • (2009) Nature , vol.460 , pp. 529-533
    • Suzuki, H.I.1    Yamagata, K.2    Sugimoto, K.3
  • 19
    • 0034703869 scopus 로고    scopus 로고
    • Dominant phenotypes produced by the HD mutation in STHdh (Q111) striatal cells
    • Trettel F., Rigamonti D., Hilditch-Maguire P., et al. Dominant phenotypes produced by the HD mutation in STHdh (Q111) striatal cells. Hum. Mol. Genet. 9 (2000) 2799-2809
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2799-2809
    • Trettel, F.1    Rigamonti, D.2    Hilditch-Maguire, P.3
  • 20
    • 42449098100 scopus 로고    scopus 로고
    • Normalization of microRNA expression levels in quantitative RT-PCR assays: identification of suitable reference RNA targets in normal and cancerous human solid tissues
    • Peltier H.J., and Latham G.J. Normalization of microRNA expression levels in quantitative RT-PCR assays: identification of suitable reference RNA targets in normal and cancerous human solid tissues. RNA 14 (2008) 844-852
    • (2008) RNA , vol.14 , pp. 844-852
    • Peltier, H.J.1    Latham, G.J.2
  • 21
    • 58149186499 scopus 로고    scopus 로고
    • MiRecords: an integrated resource for microRNA-target interactions
    • Xiao F., Zuo Z., Cai G., et al. MiRecords: an integrated resource for microRNA-target interactions. Nucl. Acids Res. 37 (2009) D105-D110
    • (2009) Nucl. Acids Res. , vol.37
    • Xiao, F.1    Zuo, Z.2    Cai, G.3
  • 22
    • 33747608638 scopus 로고    scopus 로고
    • NF-kappaB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses
    • Taganov K.D., Boldin M.P., Chang K.J., et al. NF-kappaB-dependent induction of microRNA miR-146, an inhibitor targeted to signaling proteins of innate immune responses. Proc. Natl. Acad. Sci. USA 103 (2006) 12481-12486
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12481-12486
    • Taganov, K.D.1    Boldin, M.P.2    Chang, K.J.3
  • 23
    • 29144470346 scopus 로고    scopus 로고
    • Real-time quantification of microRNAs by stem-loop RT-PCR
    • Chen C., Ridzon D.A., Broomer A.J., et al. Real-time quantification of microRNAs by stem-loop RT-PCR. Nucl. Acids Res. 33 (2005) e179
    • (2005) Nucl. Acids Res. , vol.33
    • Chen, C.1    Ridzon, D.A.2    Broomer, A.J.3
  • 24
    • 0346749473 scopus 로고    scopus 로고
    • Enhanced Akt signaling is an early pro-survival response that reflects N-methyl-d-aspartate receptor activation in Huntington's disease knock-in striatal cells
    • Gines S., Ivanova E., Seong I.S., et al. Enhanced Akt signaling is an early pro-survival response that reflects N-methyl-d-aspartate receptor activation in Huntington's disease knock-in striatal cells. J. Biol. Chem. 278 (2003) 50514-50522
    • (2003) J. Biol. Chem. , vol.278 , pp. 50514-50522
    • Gines, S.1    Ivanova, E.2    Seong, I.S.3
  • 25
    • 0037335074 scopus 로고    scopus 로고
    • Specific progressive cAMP reduction implicates energy deficit in presymptomatic Huntington's disease knock-in mice
    • Gines S., Seong I.S., Fossale E., et al. Specific progressive cAMP reduction implicates energy deficit in presymptomatic Huntington's disease knock-in mice. Hum. Mol. Genet. 12 (2003) 497-508
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 497-508
    • Gines, S.1    Seong, I.S.2    Fossale, E.3
  • 26
    • 34548399406 scopus 로고    scopus 로고
    • Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism
    • Lee J.M., Ivanova E.V., Seong I.S., et al. Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism. PLoS Genet. 3 8 (2007) e135
    • (2007) PLoS Genet. , vol.3 , Issue.8
    • Lee, J.M.1    Ivanova, E.V.2    Seong, I.S.3
  • 27
    • 54449092109 scopus 로고    scopus 로고
    • Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease
    • Quintanilla R.A., Jin Y.N., Fuenzalida K., et al. Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease. J. Biol. Chem. 283 (2008) 25628-25637
    • (2008) J. Biol. Chem. , vol.283 , pp. 25628-25637
    • Quintanilla, R.A.1    Jin, Y.N.2    Fuenzalida, K.3
  • 28
    • 43549092044 scopus 로고    scopus 로고
    • Calcineurin is involved in the early activation of NMDA-mediated cell death in mutant huntingtin knock-in striatal cells
    • Xifró X., García-Martínez J.M., Del Toro D., et al. Calcineurin is involved in the early activation of NMDA-mediated cell death in mutant huntingtin knock-in striatal cells. J. Neurochem. 105 (2008) 596-612
    • (2008) J. Neurochem. , vol.105 , pp. 596-612
    • Xifró, X.1    García-Martínez, J.M.2    Del Toro, D.3
  • 29
    • 60849125108 scopus 로고    scopus 로고
    • Increased expression of Bim contributes to the potentiation of serum deprivation-induced apoptotic cell death in Huntington's disease knock-in striatal cell line
    • Kong P.J., Kil M.O., Lee H., et al. Increased expression of Bim contributes to the potentiation of serum deprivation-induced apoptotic cell death in Huntington's disease knock-in striatal cell line. Neurol. Res. 31 (2009) 77-83
    • (2009) Neurol. Res. , vol.31 , pp. 77-83
    • Kong, P.J.1    Kil, M.O.2    Lee, H.3
  • 30
    • 66749167799 scopus 로고    scopus 로고
    • Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity
    • Subramaniam S., Sixt K.M., Barrow R., et al. Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity. Science 324 (2009) 1327-1330
    • (2009) Science , vol.324 , pp. 1327-1330
    • Subramaniam, S.1    Sixt, K.M.2    Barrow, R.3
  • 31
    • 33750432857 scopus 로고    scopus 로고
    • Comparative sequence analysis reveals an intricate network among REST, CREB and miRNA in mediating neuronal gene expression
    • Wu J., and Xie X. Comparative sequence analysis reveals an intricate network among REST, CREB and miRNA in mediating neuronal gene expression. Genome Biol. 7 (2006) R85
    • (2006) Genome Biol. , vol.7
    • Wu, J.1    Xie, X.2
  • 32
    • 34250868124 scopus 로고    scopus 로고
    • Differential regulation of microRNAs by p53 revealed by massively parallel sequencing: miR-34a is a p53 target that induces apoptosis and G1-arrest
    • Tarasov V., Jung P., Verdoodt B., et al. Differential regulation of microRNAs by p53 revealed by massively parallel sequencing: miR-34a is a p53 target that induces apoptosis and G1-arrest. Cell Cycle 6 (2007) 1586-1593
    • (2007) Cell Cycle , vol.6 , pp. 1586-1593
    • Tarasov, V.1    Jung, P.2    Verdoodt, B.3
  • 33
    • 21544450545 scopus 로고    scopus 로고
    • p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease
    • Bae B.I., Xu H., Igarashi S., et al. p53 mediates cellular dysfunction and behavioral abnormalities in Huntington's disease. Neuron 47 (2005) 29-41
    • (2005) Neuron , vol.47 , pp. 29-41
    • Bae, B.I.1    Xu, H.2    Igarashi, S.3
  • 34
    • 0032450856 scopus 로고    scopus 로고
    • Amyloid formation by mutant huntingtin: threshold, progressivity and recruitment of normal polyglutamine proteins
    • Huang C.C., Faber P.W., Persichetti F., et al. Amyloid formation by mutant huntingtin: threshold, progressivity and recruitment of normal polyglutamine proteins. Somat. Cell Mol. Genet. 24 (1998) 217-233
    • (1998) Somat. Cell Mol. Genet. , vol.24 , pp. 217-233
    • Huang, C.C.1    Faber, P.W.2    Persichetti, F.3
  • 35
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation
    • Schaffar G., Breuer P., Boteva R., et al. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol. Cell 15 (2004) 95-105
    • (2004) Mol. Cell , vol.15 , pp. 95-105
    • Schaffar, G.1    Breuer, P.2    Boteva, R.3
  • 36
    • 0036796287 scopus 로고    scopus 로고
    • Suppression of polyglutamine toxicity by a Drosophila homolog of myeloid leukemia factor 1
    • Kazemi-Esfarjani P., and Benzer S. Suppression of polyglutamine toxicity by a Drosophila homolog of myeloid leukemia factor 1. Hum. Mol. Genet. 11 (2002) 2657-2672
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2657-2672
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 37
    • 0034783914 scopus 로고    scopus 로고
    • CAG repeat expansion in the TATA box-binding protein gene causes autosomal dominant cerebellar ataxia
    • Fujigasaki H., De Martin J., Deyn P.P., et al. CAG repeat expansion in the TATA box-binding protein gene causes autosomal dominant cerebellar ataxia. Brain 124 (2001) 1939-1947
    • (2001) Brain , vol.124 , pp. 1939-1947
    • Fujigasaki, H.1    De Martin, J.2    Deyn, P.P.3
  • 38
    • 36448930958 scopus 로고    scopus 로고
    • Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration
    • Friedman M.J., Shah A.G., Fang Z.H., et al. Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration. Nat. Neurosci. 10 (2007) 1519-1528
    • (2007) Nat. Neurosci. , vol.10 , pp. 1519-1528
    • Friedman, M.J.1    Shah, A.G.2    Fang, Z.H.3
  • 39
    • 43749091298 scopus 로고    scopus 로고
    • Polyglutamine expansion reduces the association of TATA-binding protein with DNA and induces DNA binding-independent neurotoxicity
    • Friedman M.J., Wang C.E., Li X.J., and Li S. Polyglutamine expansion reduces the association of TATA-binding protein with DNA and induces DNA binding-independent neurotoxicity. J. Biol. Chem. 283 (2008) 8283-8290
    • (2008) J. Biol. Chem. , vol.283 , pp. 8283-8290
    • Friedman, M.J.1    Wang, C.E.2    Li, X.J.3    Li, S.4


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