메뉴 건너뛰기




Volumn 20, Issue 12, 2011, Pages 2308-2321

Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; PROTEASOME; TAR DNA BINDING PROTEIN;

EID: 79957488875     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddr124     Document Type: Article
Times cited : (129)

References (55)
  • 1
    • 49249118746 scopus 로고    scopus 로고
    • TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander
    • Banks, G.T., Kuta, A., Isaacs, A.M. and Fisher, E.M. (2008) TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander. Mamm. Genome, 19, 299-305.
    • (2008) Mamm. Genome , vol.19 , pp. 299-305
    • Banks, G.T.1    Kuta, A.2    Isaacs, A.M.3    Fisher, E.M.4
  • 4
    • 61549122708 scopus 로고    scopus 로고
    • Genetic studies of amyotrophic lateral sclerosis: controversies and perspectives
    • Beleza-Meireles, A. and Al-Chalabi, A. (2009) Genetic studies of amyotrophic lateral sclerosis: controversies and perspectives. Amyotroph. Lateral Scler., 10, 1-14.
    • (2009) Amyotroph. Lateral Scler. , vol.10 , pp. 1-14
    • Beleza-Meireles, A.1    Al-Chalabi, A.2
  • 7
    • 62149141328 scopus 로고    scopus 로고
    • Rethinking ALS: the FUS about TDP-43
    • Lagier-Tourenne, C. and Cleveland, D.W. (2009) Rethinking ALS: the FUS about TDP-43. Cell, 136, 1001-1004.
    • (2009) Cell , vol.136 , pp. 1001-1004
    • Lagier-Tourenne, C.1    Cleveland, D.W.2
  • 9
    • 70449698510 scopus 로고    scopus 로고
    • TDP-43 is consistently co-localized with ubiquitinated inclusions in sporadic and Guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations
    • Maekawa, S., Leigh, P.N., King, A., Jones, E., Steele, J.C., Bodi, I., Shaw, C.E., Hortobagyi, T. and Al-Sarraj, S. (2009) TDP-43 is consistently co-localized with ubiquitinated inclusions in sporadic and Guam amyotrophic lateral sclerosis but not in familial amyotrophic lateral sclerosis with and without SOD1 mutations. Neuropathology, 29, 672-683.
    • (2009) Neuropathology , vol.29 , pp. 672-683
    • Maekawa, S.1    Leigh, P.N.2    King, A.3    Jones, E.4    Steele, J.C.5    Bodi, I.6    Shaw, C.E.7    Hortobagyi, T.8    Al-Sarraj, S.9
  • 10
    • 34247606414 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation
    • Tan, C.F., Eguchi, H., Tagawa, A., Onodera, O., Iwasaki, T., Tsujino, A., Nishizawa, M., Kakita, A. and Takahashi, H. (2007) TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol., 113, 535-542.
    • (2007) Acta Neuropathol. , vol.113 , pp. 535-542
    • Tan, C.F.1    Eguchi, H.2    Tagawa, A.3    Onodera, O.4    Iwasaki, T.5    Tsujino, A.6    Nishizawa, M.7    Kakita, A.8    Takahashi, H.9
  • 16
    • 61849158637 scopus 로고    scopus 로고
    • TDP-43 neuropathology is similar in sporadic amyotrophic lateral sclerosis with or without TDP-43 mutations
    • Pamphlett, R., Luquin, N., McLean, C., Jew, S.K. and Adams, L. (2009) TDP-43 neuropathology is similar in sporadic amyotrophic lateral sclerosis with or without TDP-43 mutations. Neuropathol. Appl. Neurobiol., 35, 222-225.
    • (2009) Neuropathol. Appl. Neurobiol. , vol.35 , pp. 222-225
    • Pamphlett, R.1    Luquin, N.2    McLean, C.3    Jew, S.K.4    Adams, L.5
  • 19
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • Johnson, B.S., McCaffery, J.M., Lindquist, S. and Gitler, A.D. (2008) A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc. Natl Acad. Sci. USA, 105, 6439-6444.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 6439-6444
    • Johnson, B.S.1    McCaffery, J.M.2    Lindquist, S.3    Gitler, A.D.4
  • 20
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti, E. and Baralle, F.E. (2001) Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem., 276, 36337-36343.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 21
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang, I.F., Wu, L.S., Chang, H.Y. and Shen, C.K. (2008) TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J. Neurochem., 105, 797-806.
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1    Wu, L.S.2    Chang, H.Y.3    Shen, C.K.4
  • 24
    • 77951236534 scopus 로고    scopus 로고
    • Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS)
    • Hanson, K.A., Kim, S.H., Wassarman, D.A. and Tibbetts, R.S. (2010) Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS). J. Biol. Chem., 285, 11068-11072.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11068-11072
    • Hanson, K.A.1    Kim, S.H.2    Wassarman, D.A.3    Tibbetts, R.S.4
  • 25
    • 67349271683 scopus 로고    scopus 로고
    • Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior
    • Feiguin, F., Godena, V.K., Romano, G., D'Ambrogio, A., Klima, R. and Baralle, F.E. (2009) Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior. FEBS Lett., 583, 1586-1592.
    • (2009) FEBS Lett. , vol.583 , pp. 1586-1592
    • Feiguin, F.1    Godena, V.K.2    Romano, G.3    D'Ambrogio, A.4    Klima, R.5    Baralle, F.E.6
  • 26
    • 70350356317 scopus 로고    scopus 로고
    • Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching
    • Lu, Y., Ferris, J. and Gao, F.B. (2009) Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching. Mol. Brain, 2, 30.
    • (2009) Mol. Brain , vol.2 , pp. 30
    • Lu, Y.1    Ferris, J.2    Gao, F.B.3
  • 28
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska, I., Bell, S., Cairns, N.J., Miller, T.M. and Baloh, R.H. (2009) TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA, 106, 18809-18814.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 30
    • 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
  • 31
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H. 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.H.1    Perrimon, N.2
  • 33
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone and ALS-linked mutations accelerate aggregation and increase toxicity
    • Johnson, B.S., Snead, D., Lee, J.J., McCaffery, J.M., Shorter, J. and Gitler, A.D. (2009) TDP-43 is intrinsically aggregation-prone and ALS-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem., 284, 20329-20339.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5    Gitler, A.D.6
  • 34
    • 77949707186 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
  • 35
    • 0030087911 scopus 로고    scopus 로고
    • Distinct expression patterns detected within individual tissues by the GAL4 enhancer trap technique
    • Gustafson, K. and Boulianne, G.L. (1996) Distinct expression patterns detected within individual tissues by the GAL4 enhancer trap technique. Genome, 39, 174-182.
    • (1996) Genome , vol.39 , pp. 174-182
    • Gustafson, K.1    Boulianne, G.L.2
  • 36
    • 0008591109 scopus 로고    scopus 로고
    • Drosophila larval neuromuscular junction: molecular components and mechanisms underlying synaptic plasticity
    • Koh, Y.H., Gramates, L.S. and Budnik, V. (2000) Drosophila larval neuromuscular junction: molecular components and mechanisms underlying synaptic plasticity. Microsc. Res. Tech., 49, 14-25.
    • (2000) Microsc. Res. Tech. , vol.49 , pp. 14-25
    • Koh, Y.H.1    Gramates, L.S.2    Budnik, V.3
  • 37
    • 0031916186 scopus 로고    scopus 로고
    • Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling
    • Ranjan, R., Bronk, P. and Zinsmaier, K.E. (1998) Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling. J. Neurosci., 18, 956-964.
    • (1998) J. Neurosci. , vol.18 , pp. 956-964
    • Ranjan, R.1    Bronk, P.2    Zinsmaier, K.E.3
  • 38
    • 23944519706 scopus 로고    scopus 로고
    • LIM Kinase1 controls synaptic stability downstream of the type II BMP receptor
    • Eaton, B.A. and Davis, G.W. (2005) LIM Kinase1 controls synaptic stability downstream of the type II BMP receptor. Neuron, 47, 695-708.
    • (2005) Neuron , vol.47 , pp. 695-708
    • Eaton, B.A.1    Davis, G.W.2
  • 39
    • 0035341502 scopus 로고    scopus 로고
    • A novel member of the Ig superfamily, turtle, is a CNS-specific protein required for coordinated motor control
    • Bodily, K.D., Morrison, C.M., Renden, R.B. and Broadie, K. (2001) A novel member of the Ig superfamily, turtle, is a CNS-specific protein required for coordinated motor control. J. Neurosci., 21, 3113-3125.
    • (2001) J. Neurosci. , vol.21 , pp. 3113-3125
    • Bodily, K.D.1    Morrison, C.M.2    Renden, R.B.3    Broadie, K.4
  • 40
    • 0026528074 scopus 로고
    • Hypergravity and aging in Drosophila melanogaster. 4. Climbing activity
    • Le Bourg, E. and Lints, F.A. (1992) Hypergravity and aging in Drosophila melanogaster. 4. Climbing activity. Gerontology, 38, 59-64.
    • (1992) Gerontology , vol.38 , pp. 59-64
    • Le Bourg, E.1    Lints, F.A.2
  • 41
    • 59649086176 scopus 로고    scopus 로고
    • Molecular neuropathology of TDP-43 proteinopathies
    • Neumann, M. (2009) Molecular neuropathology of TDP-43 proteinopathies. Int. J. Mol. Sci., 10, 232-246.
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 232-246
    • Neumann, M.1
  • 42
    • 0036743483 scopus 로고    scopus 로고
    • Targeted expression of dominant negative proteasome mutants in Drosophila melanogaster
    • Belote, J.M. and Fortier, E. (2002) Targeted expression of dominant negative proteasome mutants in Drosophila melanogaster. Genesis, 34, 80-82.
    • (2002) Genesis , vol.34 , pp. 80-82
    • Belote, J.M.1    Fortier, E.2
  • 43
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick, J.M., Chan, H.Y., Gray-Board, G.L., Chai, Y., Paulson, H.L. and Bonini, N.M. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat. Genet., 23, 425-428.
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 44
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck, P.K., Chan, H.Y., Trojanowski, J.Q., Lee, V.M. and Bonini, N.M. (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science, 295, 865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 45
    • 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
  • 46
    • 0031007937 scopus 로고    scopus 로고
    • Cooperative functions of the reaper and head involution defective genes in the programmed cell death of Drosophila central nervous system midline cells
    • Zhou, L., Schnitzler, A., Agapite, J., Schwartz, L.M., Steller, H. and Nambu, J.R. (1997) Cooperative functions of the reaper and head involution defective genes in the programmed cell death of Drosophila central nervous system midline cells. Proc. Natl Acad. Sci. USA, 94, 5131-5136.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5131-5136
    • Zhou, L.1    Schnitzler, A.2    Agapite, J.3    Schwartz, L.M.4    Steller, H.5    Nambu, J.R.6
  • 49
    • 79251484992 scopus 로고    scopus 로고
    • The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism
    • Yang, C., Tan, W., Whittle, C., Qiu, L., Cao, L., Akbarian, S. and Xu, Z. (2010) The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism. PLoS ONE, 5, e15878.
    • (2010) PLoS ONE , vol.5
    • Yang, C.1    Tan, W.2    Whittle, C.3    Qiu, L.4    Cao, L.5    Akbarian, S.6    Xu, Z.7
  • 55
    • 0029825051 scopus 로고    scopus 로고
    • Traffic of dynamin within individual Drosophila synaptic boutons relative to compartment-specific markers
    • Estes, P.S., Roos, J., van der Bliek, A., Kelly, R.B., Krishnan, K.S. and Ramaswami, M. (1996) Traffic of dynamin within individual Drosophila synaptic boutons relative to compartment-specific markers. J. Neurosci., 16, 5443-5456.
    • (1996) J. Neurosci. , vol.16 , pp. 5443-5456
    • Estes, P.S.1    Roos, J.2    van der Bliek, A.3    Kelly, R.B.4    Krishnan, K.S.5    Ramaswami, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.