메뉴 건너뛰기




Volumn 8, Issue 6, 2013, Pages

RNP2 of RNA Recognition Motif 1 Plays a Central Role in the Aberrant Modification of TDP-43

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEASE; RNA BINDING PROTEIN; RNP2 MOTIF OF RNA BINDING MOTIF 1 PROTEIN; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 84879523611     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066966     Document Type: Article
Times cited : (5)

References (40)
  • 1
    • 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
  • 2
    • 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
  • 5
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, et al. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 40: 572-574.
    • (2008) Nat Genet , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Spiegelman, D.4    McConkey, B.J.5
  • 6
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319: 1668-1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3    Hu, X.4    Vance, C.5
  • 7
    • 42949094584 scopus 로고    scopus 로고
    • TDP-43 mutation in familial amyotrophic lateral sclerosis
    • Yokoseki A, Shiga A, Tan CF, Tagawa A, Kaneko H, et al. (2008) TDP-43 mutation in familial amyotrophic lateral sclerosis. Ann Neurol 63: 538-542.
    • (2008) Ann Neurol , vol.63 , pp. 538-542
    • Yokoseki, A.1    Shiga, A.2    Tan, C.F.3    Tagawa, A.4    Kaneko, H.5
  • 8
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, et al. (2008) Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 64: 60-70.
    • (2008) Ann Neurol , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3    Kametani, F.4    Yoshida, M.5
  • 9
    • 58049221032 scopus 로고    scopus 로고
    • Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: implications for TDP-43 in the physiological response to neuronal injury
    • Moisse K, Volkening K, Leystra-Lantz C, Welch I, Hill T, et al. (2009) Divergent patterns of cytosolic TDP-43 and neuronal progranulin expression following axotomy: implications for TDP-43 in the physiological response to neuronal injury. Brain Res 1249: 202-211.
    • (2009) Brain Res , vol.1249 , pp. 202-211
    • Moisse, K.1    Volkening, K.2    Leystra-Lantz, C.3    Welch, I.4    Hill, T.5
  • 10
    • 70449523111 scopus 로고    scopus 로고
    • Axonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons
    • Sato T, Takeuchi S, Saito A, Ding W, Bamba H, et al. (2009) Axonal ligation induces transient redistribution of TDP-43 in brainstem motor neurons. Neuroscience 164: 1565-1578.
    • (2009) Neuroscience , vol.164 , pp. 1565-1578
    • Sato, T.1    Takeuchi, S.2    Saito, A.3    Ding, W.4    Bamba, H.5
  • 11
    • 84856574050 scopus 로고    scopus 로고
    • Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies
    • Iguchi Y, Katsuno M, Takagi S, Ishigaki S, Niwa J, et al. (2012) Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies. Neurobiol Dis 45: 862-870.
    • (2012) Neurobiol Dis , vol.45 , pp. 862-870
    • Iguchi, Y.1    Katsuno, M.2    Takagi, S.3    Ishigaki, S.4    Niwa, J.5
  • 12
    • 80054714793 scopus 로고    scopus 로고
    • Cell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: implications in ALS
    • Ayala V, Granado-Serrano AB, Cacabelos D, Naudi A, Ilieva EV, et al. (2011) Cell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: implications in ALS. Acta Neuropathol 122: 259-270.
    • (2011) Acta Neuropathol , vol.122 , pp. 259-270
    • Ayala, V.1    Granado-Serrano, A.B.2    Cacabelos, D.3    Naudi, A.4    Ilieva, E.V.5
  • 14
    • 72649087184 scopus 로고    scopus 로고
    • Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
    • Wang X, Fan H, Ying Z, Li B, Wang H, et al. (2010) Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system. Neurosci Lett 469: 112-116.
    • (2010) Neurosci Lett , vol.469 , pp. 112-116
    • Wang, X.1    Fan, H.2    Ying, Z.3    Li, B.4    Wang, H.5
  • 15
    • 79960904538 scopus 로고    scopus 로고
    • Cytoplasmic accumulation and aggregation of TDP-43 upon proteasome inhibition in cultured neurons
    • van Eersel J, Ke YD, Gladbach A, Bi M, Gotz J, et al. (2011) Cytoplasmic accumulation and aggregation of TDP-43 upon proteasome inhibition in cultured neurons. PLoS One 6: e22850.
    • (2011) PLoS One , vol.6
    • van Eersel, J.1    Ke, Y.D.2    Gladbach, A.3    Bi, M.4    Gotz, J.5
  • 16
    • 84871150225 scopus 로고    scopus 로고
    • Motor neuron-specific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis
    • Tashiro Y, Urushitani M, Inoue H, Koike M, Uchiyama Y, et al. (2012) Motor neuron-specific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis. J Biol Chem 287: 42984-42994.
    • (2012) J Biol Chem , vol.287 , pp. 42984-42994
    • Tashiro, Y.1    Urushitani, M.2    Inoue, H.3    Koike, M.4    Uchiyama, Y.5
  • 17
    • 80054837386 scopus 로고    scopus 로고
    • A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD
    • Renton AE, Majounie E, Waite A, Simon-Sanchez J, Rollinson S, et al. (2011) A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72: 257-268.
    • (2011) Neuron , vol.72 , pp. 257-268
    • Renton, A.E.1    Majounie, E.2    Waite, A.3    Simon-Sanchez, J.4    Rollinson, S.5
  • 18
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez M, Mackenzie IR, Boeve BF, Boxer AL, Baker M, et al. (2011) Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72: 245-256.
    • (2011) Neuron , vol.72 , pp. 245-256
    • DeJesus-Hernandez, M.1    Mackenzie, I.R.2    Boeve, B.F.3    Boxer, A.L.4    Baker, M.5
  • 19
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, et al. (2011) Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 477: 211-215.
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1    Chen, W.2    Hong, S.T.3    Boycott, K.M.4    Gorrie, G.H.5
  • 21
    • 33750590113 scopus 로고    scopus 로고
    • The neuropathology of frontotemporal lobar degeneration caused by mutations in the progranulin gene
    • Mackenzie IR, Baker M, Pickering-Brown S, Hsiung GY, Lindholm C, et al. (2006) The neuropathology of frontotemporal lobar degeneration caused by mutations in the progranulin gene. Brain 129: 3081-3090.
    • (2006) Brain , vol.129 , pp. 3081-3090
    • Mackenzie, I.R.1    Baker, M.2    Pickering-Brown, S.3    Hsiung, G.Y.4    Lindholm, C.5
  • 22
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurin in amyotrophic lateral sclerosis
    • Maruyama H, Morino H, Ito H, Izumi Y, Kato H, et al. (2010) Mutations of optineurin in amyotrophic lateral sclerosis. Nature 465: 223-226.
    • (2010) Nature , vol.465 , pp. 223-226
    • Maruyama, H.1    Morino, H.2    Ito, H.3    Izumi, Y.4    Kato, H.5
  • 23
    • 0026465350 scopus 로고
    • Neuroblastoma x spinal cord (NSC) hybrid cell lines resemble developing motor neurons
    • Cashman NR, Durham HD, Blusztajn JK, Oda K, Tabira T, et al. (1992) Neuroblastoma x spinal cord (NSC) hybrid cell lines resemble developing motor neurons. Dev Dyn 194: 209-221.
    • (1992) Dev Dyn , vol.194 , pp. 209-221
    • Cashman, N.R.1    Durham, H.D.2    Blusztajn, J.K.3    Oda, K.4    Tabira, T.5
  • 24
    • 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
  • 25
    • 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 AM, Shankaran SS, Rodde R, 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
  • 26
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • Nonaka T, Kametani F, Arai T, Akiyama H, Hasegawa M, (2009) Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum Mol Genet 18: 3353-3364.
    • (2009) Hum Mol Genet , vol.18 , pp. 3353-3364
    • Nonaka, T.1    Kametani, F.2    Arai, T.3    Akiyama, H.4    Hasegawa, M.5
  • 28
    • 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, et al. (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
  • 29
    • 34249751076 scopus 로고    scopus 로고
    • TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein
    • Strong MJ, Volkening K, Hammond R, Yang W, Strong W, et al. (2007) TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein. Mol Cell Neurosci 35: 320-327.
    • (2007) Mol Cell Neurosci , vol.35 , pp. 320-327
    • Strong, M.J.1    Volkening, K.2    Hammond, R.3    Yang, W.4    Strong, W.5
  • 30
    • 73949134014 scopus 로고    scopus 로고
    • Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)
    • Volkening K, Leystra-Lantz C, Yang W, Jaffee H, Strong MJ, (2009) Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS). Brain Res 1305: 168-182.
    • (2009) Brain Res , vol.1305 , pp. 168-182
    • Volkening, K.1    Leystra-Lantz, C.2    Yang, W.3    Jaffee, H.4    Strong, M.J.5
  • 31
    • 73649148708 scopus 로고    scopus 로고
    • Characterization of alternative isoforms and inclusion body of the TAR DNA-binding protein-43
    • Nishimoto Y, Ito D, Yagi T, Nihei Y, Tsunoda Y, et al. (2010) Characterization of alternative isoforms and inclusion body of the TAR DNA-binding protein-43. J Biol Chem 285: 608-619.
    • (2010) J Biol Chem , vol.285 , pp. 608-619
    • Nishimoto, Y.1    Ito, D.2    Yagi, T.3    Nihei, Y.4    Tsunoda, Y.5
  • 32
    • 78149461229 scopus 로고    scopus 로고
    • Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue
    • Liu-Yesucevitz L, Bilgutay A, Zhang YJ, Vanderweyde T, Citro A, et al. (2010) Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS One 5: e13250.
    • (2010) PLoS One , vol.5
    • Liu-Yesucevitz, L.1    Bilgutay, A.2    Zhang, Y.J.3    Vanderweyde, T.4    Citro, A.5
  • 33
    • 79956304001 scopus 로고    scopus 로고
    • A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport
    • Pesiridis GS, Tripathy K, Tanik S, Trojanowski JQ, Lee VM, (2011) A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport. J Biol Chem 286: 18845-18855.
    • (2011) J Biol Chem , vol.286 , pp. 18845-18855
    • Pesiridis, G.S.1    Tripathy, K.2    Tanik, S.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 34
    • 77957918535 scopus 로고    scopus 로고
    • TDP-43-mediated neuron loss in vivo requires RNA-binding activity
    • Voigt A, Herholz D, Fiesel FC, Kaur K, Muller D, et al. (2010) TDP-43-mediated neuron loss in vivo requires RNA-binding activity. PLoS One 5: e12247.
    • (2010) PLoS One , vol.5
    • Voigt, A.1    Herholz, D.2    Fiesel, F.C.3    Kaur, K.4    Muller, D.5
  • 35
    • 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
  • 36
    • 50549103984 scopus 로고    scopus 로고
    • Protein solubility and folding enhancement by interaction with RNA
    • Choi SI, Han KS, Kim CW, Ryu KS, Kim BH, et al. (2008) Protein solubility and folding enhancement by interaction with RNA. PLoS One 3: e2677.
    • (2008) PLoS One , vol.3
    • Choi, S.I.1    Han, K.S.2    Kim, C.W.3    Ryu, K.S.4    Kim, B.H.5
  • 37
    • 0016262065 scopus 로고
    • Motor neurone disease: the nature of the pathogenic mechanism
    • Mann DMA, Yates P, (1974) Motor neurone disease: the nature of the pathogenic mechanism. J Neurol Neurosurg Psychiatry 37: 1036-1046.
    • (1974) J Neurol Neurosurg Psychiatry , vol.37 , pp. 1036-1046
    • Mann, D.M.A.1    Yates, P.2
  • 38
    • 77951183978 scopus 로고    scopus 로고
    • Prion-like disorders: blurring the divide between transmissibility and infectivity
    • Cushman M, Johnson BS, King OD, Gitler AD, Shorter J, (2010) Prion-like disorders: blurring the divide between transmissibility and infectivity. J Cell Sci 123: 1191-1201.
    • (2010) J Cell Sci , vol.123 , pp. 1191-1201
    • Cushman, M.1    Johnson, B.S.2    King, O.D.3    Gitler, A.D.4    Shorter, J.5
  • 39
    • 84860271370 scopus 로고    scopus 로고
    • The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies
    • Wang IF, Chang HY, Hou SC, Liou GG, Way TD, et al. (2012) The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies. Nat Commun 3: 766.
    • (2012) Nat Commun , vol.3 , pp. 766
    • Wang, I.F.1    Chang, H.Y.2    Hou, S.C.3    Liou, G.G.4    Way, T.D.5
  • 40
    • 77956155794 scopus 로고    scopus 로고
    • Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43
    • Fuentealba RA, Udan M, Bell S, Wegorzewska I, Shao J, et al. (2010) Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43. J Biol Chem 285: 26304-26314.
    • (2010) J Biol Chem , vol.285 , pp. 26304-26314
    • Fuentealba, R.A.1    Udan, M.2    Bell, S.3    Wegorzewska, I.4    Shao, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.