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Volumn 17, Issue 3, 2008, Pages 376-390

Comparative analysis of genetic modifiers in drosophila points to common and distinct mechanisms of pathogenesis among polyglutamine diseases

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 1; HUNTINGTIN;

EID: 38349171781     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddm315     Document Type: Article
Times cited : (66)

References (49)
  • 1
    • 34547692622 scopus 로고    scopus 로고
    • Trinucleotide repeat disorders
    • Orr, H.T. and Zoghbi, H.Y. (2007) Trinucleotide repeat disorders. Annu. Rev. Neurosci., 30, 575-621.
    • (2007) Annu. Rev. Neurosci , vol.30 , pp. 575-621
    • Orr, H.T.1    Zoghbi, H.Y.2
  • 2
    • 0036720019 scopus 로고    scopus 로고
    • Mouse and fly models of neurodegeneration
    • Zoghbi, H.Y. and Botas, J. (2002) Mouse and fly models of neurodegeneration. Trends Genet., 18, 463-471.
    • (2002) Trends Genet , vol.18 , pp. 463-471
    • Zoghbi, H.Y.1    Botas, J.2
  • 3
    • 25844487226 scopus 로고    scopus 로고
    • Diseases of unstable repeat expansion: Mechanisms and common principles
    • Gatchel, J.R. and Zoghbi, H.Y. (2005) Diseases of unstable repeat expansion: Mechanisms and common principles. Nat. Rev. Genet., 6, 743-755.
    • (2005) Nat. Rev. Genet , vol.6 , pp. 743-755
    • Gatchel, J.R.1    Zoghbi, H.Y.2
  • 4
    • 28644433087 scopus 로고    scopus 로고
    • Normal huntingtin function: An alternative approach to Huntington's disease
    • Cattaneo, E., Zuccato, C. and Tartari, M. (2005) Normal huntingtin function: An alternative approach to Huntington's disease. Nat. Rev. Neurosci., 6, 919-930.
    • (2005) Nat. Rev. Neurosci , vol.6 , pp. 919-930
    • Cattaneo, E.1    Zuccato, C.2    Tartari, M.3
  • 5
    • 17844392364 scopus 로고    scopus 로고
    • The pathogenesis of spinocerebellar ataxia
    • Koeppen, A.H. (2005) The pathogenesis of spinocerebellar ataxia. Cerebellum, 4, 62-73.
    • (2005) Cerebellum , vol.4 , pp. 62-73
    • Koeppen, A.H.1
  • 6
    • 0031446233 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions: A common pathogenic mechanism for glutamine-repeat neurodegenerative diseases?
    • Ross, C.A. (1997) Intranuclear neuronal inclusions: A common pathogenic mechanism for glutamine-repeat neurodegenerative diseases? Neuron, 19, 1147-1150.
    • (1997) Neuron , vol.19 , pp. 1147-1150
    • Ross, C.A.1
  • 7
    • 0032475877 scopus 로고    scopus 로고
    • Nuclear inclusions in glutamine repeat disorders: Are they pernicious, coincidental, or beneficial? [comment]
    • Sisodia, S.S. (1998) Nuclear inclusions in glutamine repeat disorders: are they pernicious, coincidental, or beneficial? [comment]. Cell, 95, 1-4.
    • (1998) Cell , vol.95 , pp. 1-4
    • Sisodia, S.S.1
  • 8
    • 0035871295 scopus 로고    scopus 로고
    • Beyond the Qs in the polyglutamine diseases
    • Orr, H.T. (2001) Beyond the Qs in the polyglutamine diseases. Genes Dev., 15, 925-932.
    • (2001) Genes Dev , vol.15 , pp. 925-932
    • Orr, H.T.1
  • 9
    • 33747359908 scopus 로고    scopus 로고
    • Polyglutamine neurodegenerative diseases and regulation of transcription: Assembling the puzzle
    • Riley, B.E. and Orr, H.T. (2006) Polyglutamine neurodegenerative diseases and regulation of transcription: Assembling the puzzle. Genes Dev., 20, 2183-2192.
    • (2006) Genes Dev , vol.20 , pp. 2183-2192
    • Riley, B.E.1    Orr, H.T.2
  • 10
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross, C.A. (2002) Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron, 35, 819-822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 12
    • 24344461460 scopus 로고    scopus 로고
    • Synaptic dysfunction in Huntington's disease: A new perspective
    • Smith, R., Brundin, P. and Li, J.Y. (2005) Synaptic dysfunction in Huntington's disease: A new perspective. Cell. Mol. Life. Sci., 62, 1901-1912.
    • (2005) Cell. Mol. Life. Sci , vol.62 , pp. 1901-1912
    • Smith, R.1    Brundin, P.2    Li, J.Y.3
  • 13
    • 4444302167 scopus 로고    scopus 로고
    • Deranged neuronal calcium signaling and Huntington disease
    • Bezprozvanny, I. and Hayden, M.R. (2004) Deranged neuronal calcium signaling and Huntington disease. Biochem. Biophys. Res. Commun., 322, 1310-1317.
    • (2004) Biochem. Biophys. Res. Commun , vol.322 , pp. 1310-1317
    • Bezprozvanny, I.1    Hayden, M.R.2
  • 14
    • 0029175420 scopus 로고
    • Spinocerebellar ataxia type 1
    • Zoghbi, H.Y. (1995) Spinocerebellar ataxia type 1. Clin. Neurosci. 3, 5-11.
    • (1995) Clin. Neurosci , vol.3 , pp. 5-11
    • Zoghbi, H.Y.1
  • 15
    • 8844220536 scopus 로고    scopus 로고
    • Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series
    • Landles, C. and Bates, G.P. (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
  • 16
    • 0036081081 scopus 로고    scopus 로고
    • Homophila: Human disease gene cognates in Drosophila
    • Chien, S., Reiter, L.T., Bier, E. and Gribskov, M. (2002) Homophila: human disease gene cognates in Drosophila. Nucleic Acids Res., 30, 149-151.
    • (2002) Nucleic Acids Res , vol.30 , pp. 149-151
    • Chien, S.1    Reiter, L.T.2    Bier, E.3    Gribskov, M.4
  • 17
    • 5744248243 scopus 로고    scopus 로고
    • Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases
    • Ghosh, S. and Feany, M.B. (2004) Comparison of pathways controlling toxicity in the eye and brain in Drosophila models of human neurodegenerative diseases. Hum. Mol. Genet., 13, 2011-2018.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 2011-2018
    • Ghosh, S.1    Feany, M.B.2
  • 21
    • 0037201934 scopus 로고    scopus 로고
    • Current thoughts on the phosphatidylinositol transfer protein family
    • Allen-Baume, V., Segui, B. and Cockcroft, S. (2002) Current thoughts on the phosphatidylinositol transfer protein family. FEBS Lett., 531, 74-80.
    • (2002) FEBS Lett , vol.531 , pp. 74-80
    • Allen-Baume, V.1    Segui, B.2    Cockcroft, S.3
  • 22
    • 0032816908 scopus 로고    scopus 로고
    • The latest in signal transduction, 1999. Specificity in Signal Transduction, Keystone, Colorado, USA, 9-14 April 1999
    • Spana, E. and Perrimon, N. (1999) The latest in signal transduction, 1999. Specificity in Signal Transduction, Keystone, Colorado, USA, 9-14 April 1999. Trends Genet., 15, 301-302.
    • (1999) Trends Genet , vol.15 , pp. 301-302
    • Spana, E.1    Perrimon, N.2
  • 23
    • 33745511725 scopus 로고    scopus 로고
    • The Drosophila phosphatidylinositol transfer protein encoded by vibrator is essential to maintain cleavage-furrow ingression in cytokinesis
    • Gatt, M.K. and Glover, D.M. (2006) The Drosophila phosphatidylinositol transfer protein encoded by vibrator is essential to maintain cleavage-furrow ingression in cytokinesis. J. Cell Sci. 119, 2225-2235.
    • (2006) J. Cell Sci , vol.119 , pp. 2225-2235
    • Gatt, M.K.1    Glover, D.M.2
  • 25
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci., 4, 49-60.
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 26
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars, K.L. and Rubinsztein, D.C. (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
  • 27
    • 0033953015 scopus 로고    scopus 로고
    • Caspases and neurodegeneration: On the cutting edge of new therapeutic approaches
    • Wellington, C.L. and Hayden, M.R. (2000) Caspases and neurodegeneration: on the cutting edge of new therapeutic approaches. Clin. Genet., 57, 1-10.
    • (2000) Clin. Genet , vol.57 , pp. 1-10
    • Wellington, C.L.1    Hayden, M.R.2
  • 28
    • 0041880131 scopus 로고    scopus 로고
    • RNA-mediated neurodegeneration caused by the fragile X premutation rCGG repeats in Drosophila
    • Jin, P., Zarnescu, D.C., Zhang, F., Pearson, C.E., Lucchesi, J.C., Moses, K. and Warren, S.T. (2003) RNA-mediated neurodegeneration caused by the fragile X premutation rCGG repeats in Drosophila. Neuron, 39, 739-747.
    • (2003) Neuron , vol.39 , pp. 739-747
    • Jin, P.1    Zarnescu, D.C.2    Zhang, F.3    Pearson, C.E.4    Lucchesi, J.C.5    Moses, K.6    Warren, S.T.7
  • 29
    • 4444299702 scopus 로고    scopus 로고
    • Pathogenic RNA repeats: An expanding role in genetic disease
    • Ranum, L.P. and Day, J.W. (2004) Pathogenic RNA repeats: An expanding role in genetic disease. Trends Genet., 20, 506-512.
    • (2004) Trends Genet , vol.20 , pp. 506-512
    • Ranum, L.P.1    Day, J.W.2
  • 33
    • 0035168621 scopus 로고    scopus 로고
    • The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract
    • Yue, S., Serra, H.G., Zoghbi, H.Y. and Orr, H.T. (2001) The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract. Hum. Mol. Genet., 10, 25-30.
    • (2001) Hum. Mol. Genet , vol.10 , pp. 25-30
    • Yue, S.1    Serra, H.G.2    Zoghbi, H.Y.3    Orr, H.T.4
  • 34
    • 24944582633 scopus 로고    scopus 로고
    • GAPs in growth factor signalling
    • Bernards, A. and Settleman, J. (2005) GAPs in growth factor signalling. Growth Factors, 23, 143-149.
    • (2005) Growth Factors , vol.23 , pp. 143-149
    • Bernards, A.1    Settleman, J.2
  • 35
    • 9644276865 scopus 로고    scopus 로고
    • Rho GTPases regulate axon growth through convergent and divergent signaling pathways
    • Ng, J. and Luo, L. (2004) Rho GTPases regulate axon growth through convergent and divergent signaling pathways. Neuron, 44, 779-793.
    • (2004) Neuron , vol.44 , pp. 779-793
    • Ng, J.1    Luo, L.2
  • 36
    • 33745103749 scopus 로고    scopus 로고
    • Does isoform diversity explain functional differences in the 14-3-3 protein family?
    • Kjarland, E., Keen, T.J. and Kleppe, R. (2006) Does isoform diversity explain functional differences in the 14-3-3 protein family? Curr. Pharm. Biotechnol., 7, 217-223.
    • (2006) Curr. Pharm. Biotechnol , vol.7 , pp. 217-223
    • Kjarland, E.1    Keen, T.J.2    Kleppe, R.3
  • 37
    • 0034754875 scopus 로고    scopus 로고
    • Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation
    • Waelter, S., Boeddrich, A., Lurz, R., Scherzinger, E., Lueder, G., Lehrach, H. and Wanker, E.E. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol. Biol. Cell, 12, 1393-1407.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1393-1407
    • Waelter, S.1    Boeddrich, A.2    Lurz, R.3    Scherzinger, E.4    Lueder, G.5    Lehrach, H.6    Wanker, E.E.7
  • 38
    • 33947511907 scopus 로고    scopus 로고
    • 14-3-3 protein interacts with Huntinglin-associated. protein I and regulates its trafficking
    • Rong, J., Li, S., Sheng, G., Wu, M., Coblitz, B., Li, M., Fu, H. and Li, X.J. (2007) 14-3-3 protein interacts with Huntinglin-associated. protein I and regulates its trafficking. J. Biol. Chem., 282, 4749-4756.
    • (2007) J. Biol. Chem , vol.282 , pp. 4749-4756
    • Rong, J.1    Li, S.2    Sheng, G.3    Wu, M.4    Coblitz, B.5    Li, M.6    Fu, H.7    Li, X.J.8
  • 39
    • 0842265636 scopus 로고    scopus 로고
    • The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin
    • Rangone, H., Poizat, G., Troncoso, J., Ross, C.A., MacDonald, M.E., Saudou, F. and Humbert, S. (2004) The serum- and glucocorticoid-induced kinase SGK inhibits mutant huntingtin-induced toxicity by phosphorylating serine 421 of huntingtin. Eur. J. Neurosci., 19 273-279.
    • (2004) Eur. J. Neurosci , vol.19 , pp. 273-279
    • Rangone, H.1    Poizat, G.2    Troncoso, J.3    Ross, C.A.4    MacDonald, M.E.5    Saudou, F.6    Humbert, S.7
  • 40
    • 20444455430 scopus 로고    scopus 로고
    • Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment
    • Rangone, H., Pardo, R., Colin, E., Girault, J.A., Saudou, F. and Humbert, S. (2005) Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment. J. Biol. Chem., 280, 22021-22028.
    • (2005) J. Biol. Chem , vol.280 , pp. 22021-22028
    • Rangone, H.1    Pardo, R.2    Colin, E.3    Girault, J.A.4    Saudou, F.5    Humbert, S.6
  • 41
    • 0036223676 scopus 로고    scopus 로고
    • The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
    • Makeyev, A.V. and Liebhaber, S.A. (2002) The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms. Rna, 8 265-278.
    • (2002) Rna , vol.8 , pp. 265-278
    • Makeyev, A.V.1    Liebhaber, S.A.2
  • 42
    • 2342618157 scopus 로고    scopus 로고
    • Biological functions of phosphatidylinositol transfer proteins
    • Routt, S.M. and Bankaitis, V.A. (2004) Biological functions of phosphatidylinositol transfer proteins. Biochem. Cell. Biol., 82, 254-262.
    • (2004) Biochem. Cell. Biol , vol.82 , pp. 254-262
    • Routt, S.M.1    Bankaitis, V.A.2
  • 43
    • 0034123912 scopus 로고    scopus 로고
    • Abnormal activity of membrane phospholipid synthetic enzymes in the brain of patients with Friedreich's ataxia and spinocerebellar atrophy type-1
    • Ross, B.M., Eder, K., Moszczynska, A., Mamalias, N., Lamarche, J., Ang, L., Pandolfo, M., Rouleau, G., Kirchgessner, M. and Kish, S.J. (2000) Abnormal activity of membrane phospholipid synthetic enzymes in the brain of patients with Friedreich's ataxia and spinocerebellar atrophy type-1. Mov. Disord., 15, 294-300.
    • (2000) Mov. Disord , vol.15 , pp. 294-300
    • Ross, B.M.1    Eder, K.2    Moszczynska, A.3    Mamalias, N.4    Lamarche, J.5    Ang, L.6    Pandolfo, M.7    Rouleau, G.8    Kirchgessner, M.9    Kish, S.J.10
  • 44
    • 3042539683 scopus 로고    scopus 로고
    • Biochemical aspects of neurodegmeration in human brain: Involvement of neural membrane phospholipids and phospholipases A2
    • Farooqui, A.A., Ong, W.Y. and Horrocks, L.A. (2004) Biochemical aspects of neurodegmeration in human brain: Involvement of neural membrane phospholipids and phospholipases A2. Neurochem. Res., 29, 1961-1977.
    • (2004) Neurochem. Res , vol.29 , pp. 1961-1977
    • Farooqui, A.A.1    Ong, W.Y.2    Horrocks, L.A.3
  • 45
    • 34548702192 scopus 로고    scopus 로고
    • Regulation of intracellular HAP1 trafficking
    • Rong, J., Li, S.H. and Li, X.J. (2007) Regulation of intracellular HAP1 trafficking. J. Neurosci. Res., 85, 3025-3029.
    • (2007) J. Neurosci. Res , vol.85 , pp. 3025-3029
    • Rong, J.1    Li, S.H.2    Li, X.J.3
  • 46
    • 33947360340 scopus 로고    scopus 로고
    • Hypothesis: Huntingtin may function in membrane association and vesicular trafficking
    • Truant, R., Atwal, R. and Burtnik A. (2006) Hypothesis: Huntingtin may function in membrane association and vesicular trafficking. Biochem. Cell. Biol., 84, 912-917.
    • (2006) Biochem. Cell. Biol , vol.84 , pp. 912-917
    • Truant, R.1    Atwal, R.2    Burtnik, A.3
  • 48
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A. and Perrimon, N. (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.1    Perrimon, N.2
  • 49
    • 0035891190 scopus 로고    scopus 로고
    • pasilla, the Drosophila homologue of the human Nova-1 and Nova-2 proteins, is required for normal secretion in the salivary gland
    • Seshaiah, P., Miller, B., Myat, M.M. and Andrew, D.J. (2001) pasilla, the Drosophila homologue of the human Nova-1 and Nova-2 proteins, is required for normal secretion in the salivary gland. Dev. Biol. 239, 309-322.
    • (2001) Dev. Biol , vol.239 , pp. 309-322
    • Seshaiah, P.1    Miller, B.2    Myat, M.M.3    Andrew, D.J.4


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