메뉴 건너뛰기




Volumn 6, Issue 6, 2011, Pages

Neuronal function and dysfunction of drosophila dTDP

Author keywords

[No Author keywords available]

Indexed keywords

TAR DNA BINDING PROTEIN; DNA BINDING PROTEIN; DROSOPHILA PROTEIN;

EID: 79957801387     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0020371     Document Type: Article
Times cited : (68)

References (39)
  • 1
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou SH, Wu F, Harrich D, Garcia-Martinez LF, Gaynor RB, (1995) Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J Virol 69: 3584-3596.
    • (1995) J Virol , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    Garcia-Martinez, L.F.4    Gaynor, R.B.5
  • 2
    • 0344256486 scopus 로고    scopus 로고
    • Structural diversity and functional implications of the eukaryotic TDP gene family
    • Wang HY, Wang IF, Bose J, Shen CK, (2004) Structural diversity and functional implications of the eukaryotic TDP gene family. Genomics 83: 130-139.
    • (2004) Genomics , vol.83 , pp. 130-139
    • Wang, H.Y.1    Wang, I.F.2    Bose, J.3    Shen, C.K.4
  • 3
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti E, Dork T, Zuccato E, Pagani F, Romano M, et al. (2001) Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J 20: 1774-1784.
    • (2001) EMBO J , vol.20 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5
  • 4
    • 57649174592 scopus 로고    scopus 로고
    • TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
    • Bose JK, Wang IF, Hung L, Tarn WY, Shen CK, (2008) TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing. J Biol Chem 283: 28852-28859.
    • (2008) J Biol Chem , vol.283 , pp. 28852-28859
    • Bose, J.K.1    Wang, I.F.2    Hung, L.3    Tarn, W.Y.4    Shen, C.K.5
  • 5
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang IF, Wu LS, Chang HY, Shen CK, (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
  • 6
    • 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, Baralle FE, (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
  • 7
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • Kuo PH, Doudeva LG, Wang YT, Shen CK, Yuan HS, (2009) Structural insights into TDP-43 in nucleic-acid binding and domain interactions. Nucleic Acids Res 37: 1799-1808.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.4    Yuan, H.S.5
  • 8
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti E, Brindisi A, Giombi M, Tisminetzky S, Ayala YM, et al. (2005) TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J Biol Chem 280: 37572-37584.
    • (2005) J Biol Chem , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5
  • 9
    • 54249100481 scopus 로고    scopus 로고
    • TDP-43: an emerging new player in neurodegenerative diseases
    • Wang IF, Wu LS, Shen CK, (2008) TDP-43: an emerging new player in neurodegenerative diseases. Trends Mol Med 14: 479-485.
    • (2008) Trends Mol Med , vol.14 , pp. 479-485
    • Wang, I.F.1    Wu, L.S.2    Shen, C.K.3
  • 10
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, et al. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351: 602-611.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5
  • 11
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, et al. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314: 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5
  • 13
    • 34848921202 scopus 로고    scopus 로고
    • Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43
    • Zhang YJ, Xu YF, Dickey CA, Buratti E, Baralle F, et al. (2007) Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. J Neurosci 27: 10530-10534.
    • (2007) J Neurosci , vol.27 , pp. 10530-10534
    • Zhang, Y.J.1    Xu, Y.F.2    Dickey, C.A.3    Buratti, E.4    Baralle, F.5
  • 14
    • 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
  • 15
  • 16
    • 67649797399 scopus 로고    scopus 로고
    • Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies
    • Igaz LM, Kwong LK, Chen-Plotkin A, Winton MJ, Unger TL, et al. (2009) Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies. J Biol Chem 284: 8516-8524.
    • (2009) J Biol Chem , vol.284 , pp. 8516-8524
    • Igaz, L.M.1    Kwong, L.K.2    Chen-Plotkin, A.3    Winton, M.J.4    Unger, T.L.5
  • 17
    • 77949908515 scopus 로고    scopus 로고
    • Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy
    • Arai T, Hasegawa M, Nonoka T, Kametani F, Yamashita M, et al. (2010) Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy. Neuropathology 30: 170-181.
    • (2010) Neuropathology , vol.30 , pp. 170-181
    • Arai, T.1    Hasegawa, M.2    Nonoka, T.3    Kametani, F.4    Yamashita, M.5
  • 18
    • 77951236534 scopus 로고    scopus 로고
    • Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS)
    • Hanson KA, Kim SH, Wassarman DA, Tibbetts RS, (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
  • 20
    • 77955395385 scopus 로고    scopus 로고
    • Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U
    • Tsai KJ, Yang CH, Fang YH, Cho KH, Chien WL, et al. (2010) Elevated expression of TDP-43 in the forebrain of mice is sufficient to cause neurological and pathological phenotypes mimicking FTLD-U. J Exp Med 207: 1661-1673.
    • (2010) J Exp Med , vol.207 , pp. 1661-1673
    • Tsai, K.J.1    Yang, C.H.2    Fang, Y.H.3    Cho, K.H.4    Chien, W.L.5
  • 21
    • 77649269011 scopus 로고    scopus 로고
    • TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
    • Wils H, Kleinberger G, Janssens J, Pereson S, Joris G, et al. (2010) TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc Natl Acad Sci USA 107: 3858-3863.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3858-3863
    • Wils, H.1    Kleinberger, G.2    Janssens, J.3    Pereson, S.4    Joris, G.5
  • 23
    • 67349271683 scopus 로고    scopus 로고
    • Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior
    • Feiguin F, Godena VK, Romano G, D'Ambrogio A, Klima R, et al. (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
  • 24
    • 70350356317 scopus 로고    scopus 로고
    • Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching
    • Lu Y, Ferris J, Gao FB, (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
  • 25
    • 0030449882 scopus 로고    scopus 로고
    • Associative learning disrupted by impaired Gs signaling in Drosophila mushroom bodies
    • Connolly JB, Roberts IJ, Armstrong JD, Kaiser K, Forte M, et al. (1996) Associative learning disrupted by impaired Gs signaling in Drosophila mushroom bodies. Science 274: 2104-2107.
    • (1996) Science , vol.274 , pp. 2104-2107
    • Connolly, J.B.1    Roberts, I.J.2    Armstrong, J.D.3    Kaiser, K.4    Forte, M.5
  • 26
    • 0034724897 scopus 로고    scopus 로고
    • Localization of a short-term memory in Drosophila
    • Zars T, Fischer M, Schulz R, Heisenberg M, (2000) Localization of a short-term memory in Drosophila. Science 288: 672-675.
    • (2000) Science , vol.288 , pp. 672-675
    • Zars, T.1    Fischer, M.2    Schulz, R.3    Heisenberg, M.4
  • 27
    • 0032821487 scopus 로고    scopus 로고
    • Development of the Drosophila mushroom bodies: sequential generation of three distinct types of neurons from a neuroblast
    • Lee T, Lee A, Luo L, (1999) Development of the Drosophila mushroom bodies: sequential generation of three distinct types of neurons from a neuroblast. Development 126: 4065-4076.
    • (1999) Development , vol.126 , pp. 4065-4076
    • Lee, T.1    Lee, A.2    Luo, L.3
  • 28
    • 77949878273 scopus 로고    scopus 로고
    • TDP-43 is a developmentally regulated protein essential for early embryonic development
    • Sephton CF, Good SK, Atkin S, Dewey CM, Mayer P 3rd, et al. (2010) TDP-43 is a developmentally regulated protein essential for early embryonic development. J Biol Chem 285: 6826-6834.
    • (2010) J Biol Chem , vol.285 , pp. 6826-6834
    • Sephton, C.F.1    Good, S.K.2    Atkin, S.3    Dewey, C.M.4    Mayer III, P.5
  • 29
    • 74749107048 scopus 로고    scopus 로고
    • TDP-43, a neuro-pathosignature factor, is essential for early mouse embryogenesis
    • Wu LS, Cheng WC, Hou SC, Yan YT, Jiang ST, et al. (2010) TDP-43, a neuro-pathosignature factor, is essential for early mouse embryogenesis. Genesis 48: 56-62.
    • (2010) Genesis , vol.48 , pp. 56-62
    • Wu, L.S.1    Cheng, W.C.2    Hou, S.C.3    Yan, Y.T.4    Jiang, S.T.5
  • 30
    • 77949897022 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: a spectrum of TDP-43 proteinopathies
    • Geser F, Lee VM, Trojanowski JQ, (2010) Amyotrophic lateral sclerosis and frontotemporal lobar degeneration: a spectrum of TDP-43 proteinopathies. Neuropathology 30: 103-112.
    • (2010) Neuropathology , vol.30 , pp. 103-112
    • Geser, F.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 31
    • 0034934752 scopus 로고    scopus 로고
    • Flies, genes, and learning
    • Waddell S, Quinn WG, (2001) Flies, genes, and learning. Annu Rev Neurosci 24: 1283-1309.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1283-1309
    • Waddell, S.1    Quinn, W.G.2
  • 32
    • 57049149602 scopus 로고    scopus 로고
    • Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis
    • Kasai T, Tokuda T, Ishigami N, Sasayama H, Foulds P, et al. (2009) Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis. Acta Neuropathol 117: 55-62.
    • (2009) Acta Neuropathol , vol.117 , pp. 55-62
    • Kasai, T.1    Tokuda, T.2    Ishigami, N.3    Sasayama, H.4    Foulds, P.5
  • 33
    • 34447099071 scopus 로고    scopus 로고
    • Gene expression analysis of frontotemporal lobar degeneration of the motor neuron disease type with ubiquitinated inclusions
    • Mishra M, Paunesku T, Woloschak GE, Siddique T, Zhu LJ, et al. (2007) Gene expression analysis of frontotemporal lobar degeneration of the motor neuron disease type with ubiquitinated inclusions. Acta Neuropathol 114: 81-94.
    • (2007) Acta Neuropathol , vol.114 , pp. 81-94
    • Mishra, M.1    Paunesku, T.2    Woloschak, G.E.3    Siddique, T.4    Zhu, L.J.5
  • 34
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska I, Bell S, Cairns NJ, Miller TM, Baloh RH, (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
  • 35
    • 77950421249 scopus 로고    scopus 로고
    • Transgenic rat model of neurodegeneration caused by mutation in the TDP gene
    • Zhou H, Huang C, Chen H, Wang D, Landel CP, et al. (2010) Transgenic rat model of neurodegeneration caused by mutation in the TDP gene. PLoS Genet 6: e1000887.
    • (2010) PLoS Genet , vol.6
    • Zhou, H.1    Huang, C.2    Chen, H.3    Wang, D.4    Landel, C.P.5
  • 36
    • 17144426507 scopus 로고    scopus 로고
    • Human, Drosophila, and C.elegans TDP43: nucleic acid binding properties and splicing regulatory function
    • Ayala YM, Pantano S, D'Ambrogio A, Buratti E, Brindisi A, et al. (2005) Human, Drosophila, and C.elegans TDP43: nucleic acid binding properties and splicing regulatory function. J Mol Biol 348: 575-588.
    • (2005) J Mol Biol , vol.348 , pp. 575-588
    • Ayala, Y.M.1    Pantano, S.2    D'Ambrogio, A.3    Buratti, E.4    Brindisi, A.5
  • 37
    • 0000064419 scopus 로고
    • Behavioral mutants of Drosophila isolated by countercurrent distribution
    • Benzer S, (1967) Behavioral mutants of Drosophila isolated by countercurrent distribution. Proc Natl Acad Sci USA 58: 1112-1119.
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 1112-1119
    • Benzer, S.1
  • 38
    • 0022119763 scopus 로고
    • Classical conditioning and retention in normal and mutant Drosophila melanogaster
    • Tully T, Quinn WG, (1985) Classical conditioning and retention in normal and mutant Drosophila melanogaster. J Comp Physiol 157: 263-277.
    • (1985) J Comp Physiol , vol.157 , pp. 263-277
    • Tully, T.1    Quinn, W.G.2
  • 39
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton MJ, Igaz LM, Wong MM, Kwong LK, Trojanowski JQ, et al. (2008) Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J Biol Chem 283: 13302-13309.
    • (2008) J Biol Chem , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.