메뉴 건너뛰기




Volumn 22, Issue 4, 2013, Pages 782-794

Reduction of polyglutamine toxicity by TDP-43, FUS and progranulin in Huntington's disease models

Author keywords

[No Author keywords available]

Indexed keywords

ATAXIN 3; FUSED IN SARCOMA PROTEIN; POLYGLUTAMINE; PROGRANULIN; SMALL INTERFERING RNA; TAR DNA BINDING PROTEIN;

EID: 84873044588     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/dds485     Document Type: Article
Times cited : (31)

References (59)
  • 1
    • 77956362155 scopus 로고    scopus 로고
    • Protein homeostasis and aging in neurodegeneration
    • Douglas, P.M. and Dillin, A. (2010) Protein homeostasis and aging in neurodegeneration. J. Cell Biol., 190, 719-729.
    • (2010) J. Cell Biol. , vol.190 , pp. 719-729
    • Douglas, P.M.1    Dillin, A.2
  • 2
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne, C., Polymenidou, M. and Cleveland, D.W. (2010) TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet., 19, R46-R64.
    • (2010) Hum. Mol. Genet. , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 4
    • 41649106307 scopus 로고    scopus 로고
    • TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression
    • Ayala, Y.M., Misteli, T. and Baralle, F.E. (2008) TDP-43 regulates retinoblastoma protein phosphorylation through the repression of cyclin-dependent kinase 6 expression. Proc. Natl Acad. Sci. USA, 105, 3785-3789.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 3785-3789
    • Ayala, Y.M.1    Misteli, T.2    Baralle, F.E.3
  • 5
    • 2442676753 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: a functional link with disease penetrance
    • Buratti, E., Brindisi, A., Pagani, F. and Baralle, F.E. (2004) Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: a functional link with disease penetrance. Am. J. Hum. Genet., 74, 1322-1325.
    • (2004) Am. J. Hum. Genet. , vol.74 , pp. 1322-1325
    • Buratti, E.1    Brindisi, A.2    Pagani, F.3    Baralle, F.E.4
  • 6
    • 71049166754 scopus 로고    scopus 로고
    • The evidence for altered RNA metabolism in amyotrophic lateral sclerosis (ALS)
    • Strong, M.J. (2010) The evidence for altered RNA metabolism in amyotrophic lateral sclerosis (ALS). J. Neurol. Sci., 288, 1-12.
    • (2010) J. Neurol. Sci. , vol.288 , pp. 1-12
    • Strong, M.J.1
  • 11
    • 84862210719 scopus 로고    scopus 로고
    • Does a loss of TDP-43 function cause neurodegeneration?
    • Xu, Z.S. (2012) Does a loss of TDP-43 function cause neurodegeneration?. Molecular neurodegeneratin, 7, 27.
    • (2012) Molecular neurodegeneratin , vol.7 , pp. 27
    • Xu, Z.S.1
  • 12
    • 84870063066 scopus 로고    scopus 로고
    • How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other?
    • Baloh, R.H. (2012) How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other? Curr. Opin. Neurol, 25, 701-707.
    • (2012) Curr. Opin. Neurol , vol.25 , pp. 701-707
    • Baloh, R.H.1
  • 16
    • 58149398638 scopus 로고    scopus 로고
    • Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease
    • Schwab, C., Arai, T., Hasegawa, M., Yu, S. and McGeer, P.L. (2008) Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of Huntington disease. J. Neuropathol. Exp. Neurol., 67, 1159-1165.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 1159-1165
    • Schwab, C.1    Arai, T.2    Hasegawa, M.3    Yu, S.4    McGeer, P.L.5
  • 17
    • 73249135817 scopus 로고    scopus 로고
    • The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases
    • Doi, H., Koyano, S., Suzuki, Y., Nukina, N. and Kuroiwa, Y. (2009) The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases. Neurosci. Res., 66, 131-133.
    • (2009) Neurosci. Res. , vol.66 , pp. 131-133
    • Doi, H.1    Koyano, S.2    Suzuki, Y.3    Nukina, N.4    Kuroiwa, Y.5
  • 19
    • 0035818590 scopus 로고    scopus 로고
    • Expanded polyglutamines in Caenorhabditis elegans cause axonal abnormalities and severe dysfunction of PLM mechanosensory neurons without cell death
    • Parker, J.A., Connolly, J.B., Wellington, C., Hayden, M., Dausset, J. and Neri, C. (2001) Expanded polyglutamines in Caenorhabditis elegans cause axonal abnormalities and severe dysfunction of PLM mechanosensory neurons without cell death. Proc. Natl Acad. Sci. USA, 98, 13318-13323.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13318-13323
    • Parker, J.A.1    Connolly, J.B.2    Wellington, C.3    Hayden, M.4    Dausset, J.5    Neri, C.6
  • 22
    • 84864606276 scopus 로고    scopus 로고
    • TDP-1/TDP-43 Regulates stress signaling and age-dependent proteotoxicity in Caenorhabditis elegans
    • Vaccaro, A., Tauffenberger, A., Ash, P.E., Carlomagno, Y., Petrucelli, L. and Parker, J.A. (2012) TDP-1/TDP-43 Regulates stress signaling and age-dependent proteotoxicity in Caenorhabditis elegans. PLoS Genet., 8, e1002806.
    • (2012) PLoS Genet. , vol.8
    • Vaccaro, A.1    Tauffenberger, A.2    Ash, P.E.3    Carlomagno, Y.4    Petrucelli, L.5    Parker, J.A.6
  • 23
    • 84863263765 scopus 로고    scopus 로고
    • Caenorhabditis elegans RNA-processing Protein TDP-1 Regulates Protein Homeostasis and Lifespan
    • Zhang, T., Hwang, H.Y., Hao, H., Talbot, C. Jr and Wang, J. (2012) Caenorhabditis elegans RNA-processing Protein TDP-1 Regulates Protein Homeostasis and Lifespan. J. Biol. Chem, 287, 8371-8382.
    • (2012) J. Biol. Chem , vol.287 , pp. 8371-8382
    • Zhang, T.1    Hwang, H.Y.2    Hao, H.3    Talbot Jr., C.4    Wang, J.5
  • 25
    • 77958604956 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA
    • Kim, S.H., Shanware, N.P., Bowler, M.J. and Tibbetts, R.S. (2010) Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. J. Biol. Chem., 285, 34097-34105.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34097-34105
    • Kim, S.H.1    Shanware, N.P.2    Bowler, M.J.3    Tibbetts, R.S.4
  • 26
    • 35948958216 scopus 로고    scopus 로고
    • HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration
    • Pandey, U.B., Batlevi, Y., Baehrecke, E.H. and Taylor, J.P. (2007) HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration. Autophagy, 3, 643-645.
    • (2007) Autophagy , vol.3 , pp. 643-645
    • Pandey, U.B.1    Batlevi, Y.2    Baehrecke, E.H.3    Taylor, J.P.4
  • 27
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata, A., Riley, B.E., Johnston, J.A. and Kopito, R.R. (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J. Biol. Chem., 280, 40282-40292.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 29
    • 80855131487 scopus 로고    scopus 로고
    • Structure, function, and mechanism of progranulin; the brain and beyond
    • Toh, H., Chitramuthu, B.P., Bennett, H.P. and Bateman, A. (2011) Structure, function, and mechanism of progranulin; the brain and beyond. J. Mol. Neurosci., 45, 538-548.
    • (2011) J. Mol. Neurosci. , vol.45 , pp. 538-548
    • Toh, H.1    Chitramuthu, B.P.2    Bennett, H.P.3    Bateman, A.4
  • 35
    • 0038039288 scopus 로고    scopus 로고
    • Polyglutamine protein aggregation and toxicity are linked to the cellular stress response
    • Cowan, K.J., Diamond, M.I. and Welch, W.J. (2003) Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Hum. Mol. Genet., 12, 1377-1391.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1377-1391
    • Cowan, K.J.1    Diamond, M.I.2    Welch, W.J.3
  • 36
    • 80053424095 scopus 로고    scopus 로고
    • The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span
    • Wang, J.W., Brent, J.R., Tomlinson, A., Shneider, N.A. and McCabe, B.D. (2011) The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span. J. Clin. Invest, 121, 4118-4126.
    • (2011) J. Clin. Invest , vol.121 , pp. 4118-4126
    • Wang, J.W.1    Brent, J.R.2    Tomlinson, A.3    Shneider, N.A.4    McCabe, B.D.5
  • 41
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
    • Barmada, S.J., Skibinski, G., Korb, E., Rao, E.J., Wu, J.Y. and Finkbeiner, S. (2010) Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J. Neurosci., 30, 639-649.
    • (2010) J. Neurosci. , vol.30 , pp. 639-649
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5    Finkbeiner, S.6
  • 42
    • 79957488875 scopus 로고    scopus 로고
    • Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS
    • Estes, P.S., Boehringer, A., Zwick, R., Tang, J.E., Grigsby, B. and Zarnescu, D.C. (2011) Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS. Hum. Mol. Genet, 20, 2308-2321.
    • (2011) Hum. Mol. Genet , vol.20 , pp. 2308-2321
    • Estes, P.S.1    Boehringer, A.2    Zwick, R.3    Tang, J.E.4    Grigsby, B.5    Zarnescu, D.C.6
  • 45
    • 78649750391 scopus 로고    scopus 로고
    • Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy
    • Liachko, N.F., Guthrie, C.R. and Kraemer, B.C. (2010) Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy. J. Neurosci., 30, 16208-16219.
    • (2010) J. Neurosci. , vol.30 , pp. 16208-16219
    • Liachko, N.F.1    Guthrie, C.R.2    Kraemer, B.C.3
  • 47
    • 79955433159 scopus 로고    scopus 로고
    • TDP-43 neurotoxicity and protein aggregation modulated by heat shock factor and insulin/IGF-1 signaling
    • Zhang, T., Mullane, P.C., Periz, G. and Wang, J. (2011) TDP-43 neurotoxicity and protein aggregation modulated by heat shock factor and insulin/IGF-1 signaling. Hum. Mol. Genet, 20, 1952-1965.
    • (2011) Hum. Mol. Genet , vol.20 , pp. 1952-1965
    • Zhang, T.1    Mullane, P.C.2    Periz, G.3    Wang, J.4
  • 49
    • 80052936462 scopus 로고    scopus 로고
    • Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
    • Swarup, V., Phaneuf, D., Bareil, C., Robertson, J., Rouleau, G.A., Kriz, J. and Julien, J.P. (2011) Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments. Brain, 134, 2610-2626.
    • (2011) Brain , vol.134 , pp. 2610-2626
    • Swarup, V.1    Phaneuf, D.2    Bareil, C.3    Robertson, J.4    Rouleau, G.A.5    Kriz, J.6    Julien, J.P.7
  • 53
    • 79251648286 scopus 로고    scopus 로고
    • Progranulin deficiency leads to enhanced cell vulnerability and TDP-43 translocation in primary neuronal cultures
    • Guo, A., Tapia, L., Bamji, S.X., Cynader, M.S. and Jia, W. (2010) Progranulin deficiency leads to enhanced cell vulnerability and TDP-43 translocation in primary neuronal cultures. Brain Res., 1366, 1-8.
    • (2010) Brain Res. , vol.1366 , pp. 1-8
    • Guo, A.1    Tapia, L.2    Bamji, S.X.3    Cynader, M.S.4    Jia, W.5
  • 54
    • 77957818067 scopus 로고    scopus 로고
    • Progranulin modulates zebrafish motoneuron development in vivo and rescues truncation defects associated with knockdown of Survival motor neuron 1
    • Chitramuthu, B.P., Baranowski, D.C., Kay, D.G., Bateman, A. and Bennett, H.P. (2010) Progranulin modulates zebrafish motoneuron development in vivo and rescues truncation defects associated with knockdown of Survival motor neuron 1. Mol. Neurodegen., 5, 41.
    • (2010) Mol. Neurodegen. , vol.5 , pp. 41
    • Chitramuthu, B.P.1    Baranowski, D.C.2    Kay, D.G.3    Bateman, A.4    Bennett, H.P.5
  • 57
    • 67650432367 scopus 로고    scopus 로고
    • Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin
    • Dormann, D., Capell, A., Carlson, A.M., Shankaran, S.S., Rodde, R., Neumann, M., Kremmer, E., Matsuwaki, T., Yamanouchi, K., Nishihara, M. et al. (2009) Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin. J. Neurochem., 110, 1082-1094.
    • (2009) J. Neurochem. , vol.110 , pp. 1082-1094
    • Dormann, D.1    Capell, A.2    Carlson, A.M.3    Shankaran, S.S.4    Rodde, R.5    Neumann, M.6    Kremmer, E.7    Matsuwaki, T.8    Yamanouchi, K.9    Nishihara, M.10
  • 58
    • 38349173569 scopus 로고    scopus 로고
    • Missense mutations in the progranulin gene linked to frontotemporal lobar degeneration with ubiquitin-immunoreactive inclusions reduce progranulin production and secretion
    • Shankaran, S.S., Capell, A., Hruscha, A.T., Fellerer, K., Neumann, M., Schmid, B. and Haass, C. (2008) Missense mutations in the progranulin gene linked to frontotemporal lobar degeneration with ubiquitin-immunoreactive inclusions reduce progranulin production and secretion. J. Biol. Chem., 283, 1744-1753.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1744-1753
    • Shankaran, S.S.1    Capell, A.2    Hruscha, A.T.3    Fellerer, K.4    Neumann, M.5    Schmid, B.6    Haass, C.7
  • 59
    • 35348913211 scopus 로고    scopus 로고
    • Huntingtin-interacting protein 1 influences worm and mouse presynaptic function and protects Caenorhabditis elegans neurons against mutant polyglutamine toxicity
    • Parker, J.A., Metzler, M., Georgiou, J., Mage, M., Roder, J.C., Rose, A.M., Hayden, M.R. and Neri, C. (2007) Huntingtin-interacting protein 1 influences worm and mouse presynaptic function and protects Caenorhabditis elegans neurons against mutant polyglutamine toxicity. J. Neurosci., 27, 11056-11064.
    • (2007) J. Neurosci. , vol.27 , pp. 11056-11064
    • Parker, J.A.1    Metzler, M.2    Georgiou, J.3    Mage, M.4    Roder, J.C.5    Rose, A.M.6    Hayden, M.R.7    Neri, C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.