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Volumn 2, Issue 1, 2014, Pages

Reducing TDP-43 aggregation does not prevent its cytotoxicity

Author keywords

Aggregation; Cell death; Peptides; TDP 43

Indexed keywords

ARSENIC TRIOXIDE; ARSENOUS ACID DERIVATIVE; DNA BINDING PROTEIN; PROTEIN BINDING; PROTEIN TDP-43;

EID: 85005790350     PISSN: None     EISSN: 20515960     Source Type: Journal    
DOI: 10.1186/20515960149     Document Type: Article
Times cited : (22)

References (41)
  • 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.: TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 2006, 351: 602-611. 10.1016/j.bbrc.2006.10.093
    • (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.: Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006, 314: 130-133. 10.1126/science.1134108
    • (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
  • 3
    • 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: Cloning and characterization of a novel cellular protein, TDP-43, that binds to Human Immunodeficiency Virus Type 1 TAR DNA sequence motifs. J Virol 1995, 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
  • 4
    • 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.: 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 2005, 280: 37572-37584. 10.1074/jbc.M505557200
    • (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
  • 5
    • 33745277599 scopus 로고    scopus 로고
    • cis-Requirement for the maintenance of round spermatid-specific transcription
    • Acharya KK, Govind CK, Shore AN, Stoler MH, Reddi PP: cis -Requirement for the maintenance of round spermatid-specific transcription. Dev Biol 2006, 295: 781-790. 10.1016/j.ydbio.2006.04.443
    • (2006) Dev Biol , vol.295 , pp. 781-790
    • Acharya, K.K.1    Govind, C.K.2    Shore, A.N.3    Stoler, M.H.4    Reddi, P.P.5
  • 6
    • 0344256486 scopus 로고    scopus 로고
    • Structural diversity and functional implications of the eukaryotic TDP gene family
    • Wang HY, Wang IF, Bose J, Shen CK: Structural diversity and functional implications of the eukaryotic TDP gene family. Genomics 2004, 83: 130-139. 10.1016/S0888-7543(03)00214-3
    • (2004) Genomics , vol.83 , pp. 130-139
    • Wang, H.Y.1    Wang, I.F.2    Bose, J.3    Shen, C.K.4
  • 7
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • Mercado PA, Ayala YM, Romano M, Buratti E, Baralle FE: Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nucleic Acids Res 2005, 33: 6000-6010. 10.1093/nar/gki897
    • (2005) Nucleic Acids Res , vol.33 , pp. 6000-6010
    • Mercado, P.A.1    Ayala, Y.M.2    Romano, M.3    Buratti, E.4    Baralle, F.E.5
  • 8
    • 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.: Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J 2001, 20: 1774-1784. 10.1093/emboj/20.7.1774
    • (2001) EMBO J , vol.20 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3    Pagani, F.4    Romano, M.5
  • 9
    • 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.: TDP43 is a human low molecular weight neurofilament (hNFL) mRNA-binding protein. Mol Cell Neurosci 2007, 35: 320-327. 10.1016/j.mcn.2007.03.007
    • (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
  • 10
    • 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 SH, Shanware NP, Bowler MJ, Tibbetts RS: Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. J Biol Chem 2010, 285: 34097-34105. 10.1074/jbc.M110.154831
    • (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
  • 11
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford NJ, Zhang YJ, Baker M, Gass JM, Finch NA, et al.: Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet 2008, 4: e1000193. 10.1371/journal.pgen.1000193
    • (2008) PLoS Genet , vol.4
    • Rutherford, N.J.1    Zhang, Y.J.2    Baker, M.3    Gass, J.M.4    Finch, N.A.5
  • 12
    • 34247625005 scopus 로고    scopus 로고
    • Ubiquitinated pathological lesions in frontotemporal lobar degeneration contain the TAR DNA-binding protein, TDP-43
    • Davidson Y, Kelley T, Mackenzie IR, Pickering-Brown S, Du Plessis D, et al.: Ubiquitinated pathological lesions in frontotemporal lobar degeneration contain the TAR DNA-binding protein, TDP-43. Acta Neuropathol 2007, 113: 521-533. 10.1007/s00401-006-0189-y
    • (2007) Acta Neuropathol , vol.113 , pp. 521-533
    • Davidson, Y.1    Kelley, T.2    Mackenzie, I.R.3    Pickering-Brown, S.4    Du Plessis, D.5
  • 13
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • Johnson BS, McCaffery JM, Lindquist S, Gitler AD: A yeast TDP-43 proteinopathy model: exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc Natl Acad Sci U S A 2008, 105: 6439-6444. 10.1073/pnas.0802082105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 6439-6444
    • Johnson, B.S.1    McCaffery, J.M.2    Lindquist, S.3    Gitler, A.D.4
  • 15
    • 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.: Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. J Neurosci 2007, 27: 10530-10534. 10.1523/JNEUROSCI.3421-07.2007
    • (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
  • 16
    • 77956199371 scopus 로고    scopus 로고
    • Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice
    • Xu YF, Gendron TF, Zhang YJ, Lin WL, D'Alton S, et al.: Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice. J Neurosci 2010, 30: 10851-10859. 10.1523/JNEUROSCI.1630-10.2010
    • (2010) J Neurosci , vol.30 , pp. 10851-10859
    • Xu, Y.F.1    Gendron, T.F.2    Zhang, Y.J.3    Lin, W.L.4    D'Alton, S.5
  • 17
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • Shan X, Chiang PM, Price DL, Wong PC: Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc Natl Acad Sci U S A 2010, 107: 16325-16330. 10.1073/pnas.1003459107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 18
    • 58149498300 scopus 로고    scopus 로고
    • Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells
    • Nonaka T, Arai T, Buratti E, Baralle FE, Akiyama H, et al.: Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett 2009, 583: 394-400. 10.1016/j.febslet.2008.12.031
    • (2009) FEBS Lett , vol.583 , pp. 394-400
    • Nonaka, T.1    Arai, T.2    Buratti, E.3    Baralle, F.E.4    Akiyama, H.5
  • 19
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha N, Anderson P: Mammalian stress granules and processing bodies. Methods Enzymol 2007, 431: 61-81.
    • (2007) Methods Enzymol , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 20
    • 0036863320 scopus 로고    scopus 로고
    • Stress granules: sites of mRNA triage that regulate mRNA stability and translatability
    • Kedersha N, Anderson P: Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans 2002, 30: 963-969.
    • (2002) Biochem Soc Trans , vol.30 , pp. 963-969
    • Kedersha, N.1    Anderson, P.2
  • 21
    • 20144378698 scopus 로고    scopus 로고
    • Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure
    • McEwen E, Kedersha N, Song B, Scheuner D, Gilks N, et al.: Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J Biol Chem 2005, 280: 16925-16933. 10.1074/jbc.M412882200
    • (2005) J Biol Chem , vol.280 , pp. 16925-16933
    • McEwen, E.1    Kedersha, N.2    Song, B.3    Scheuner, D.4    Gilks, N.5
  • 22
    • 79952589652 scopus 로고    scopus 로고
    • TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1
    • McDonald KK, Aulas A, Destroismaisons L, Pickles S, Beleac E, et al.: TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1. Hum Mol Genet 2011, 20: 1400-1410. 10.1093/hmg/ddr021
    • (2011) Hum Mol Genet , vol.20 , pp. 1400-1410
    • McDonald, K.K.1    Aulas, A.2    Destroismaisons, L.3    Pickles, S.4    Beleac, E.5
  • 23
    • 79961117695 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress
    • Meyerowitz J, Parker SJ, Vella LJ, Ng D, Price KA, et al.: C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress. Mol Neurodegeneration 2011, 6: 57. 10.1186/1750-1326-6-57
    • (2011) Mol Neurodegeneration , vol.6 , pp. 57
    • Meyerowitz, J.1    Parker, S.J.2    Vella, L.J.3    Ng, D.4    Price, K.A.5
  • 25
    • 75149155060 scopus 로고    scopus 로고
    • Oxidative stress in ALS: key role in motor neuron injury and therapeutic target
    • Barber SC, Shaw PJ: Oxidative stress in ALS: key role in motor neuron injury and therapeutic target. Free Radic Biol Med 2010, 48: 629-641. 10.1016/j.freeradbiomed.2009.11.018
    • (2010) Free Radic Biol Med , vol.48 , pp. 629-641
    • Barber, S.C.1    Shaw, P.J.2
  • 26
    • 84857124994 scopus 로고    scopus 로고
    • Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates
    • Parker SJ, Meyerowitz J, James JL, Liddell JR, Crouch PJ, et al.: Endogenous TDP-43 localized to stress granules can subsequently form protein aggregates. Neurochem Int 2012, 60: 415-424. 10.1016/j.neuint.2012.01.019
    • (2012) Neurochem Int , vol.60 , pp. 415-424
    • Parker, S.J.1    Meyerowitz, J.2    James, J.L.3    Liddell, J.R.4    Crouch, P.J.5
  • 27
    • 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 SX, Cynader MS, Jia W: Progranulin deficiency leads to enhanced cell vulnerability and TDP-43 translocation in primary neuronal cultures. Brain Res 2010, 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
  • 28
    • 84862210719 scopus 로고    scopus 로고
    • Does a loss of TDP-43 function cause neurodegeneration?
    • Xu ZS: Does a loss of TDP-43 function cause neurodegeneration? Mol Neurodegeneration 2012, 7: 27. 10.1186/1750-1326-7-27
    • (2012) Mol Neurodegeneration , vol.7 , pp. 27
    • Xu, Z.S.1
  • 29
    • 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 SJ, Skibinski G, Korb E, Rao EJ, Wu JY, et al.: Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J Neurosci 2010, 30: 639-649. 10.1523/JNEUROSCI.4988-09.2010
    • (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
  • 30
    • 79551523377 scopus 로고    scopus 로고
    • Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
    • Igaz LM, Kwong LK, Lee EB, Chen-Plotkin A, Swanson E, Unger T, Malunda J, et al.: Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice. J Clin Invest 2011, 121: 726-738. 10.1172/JCI44867
    • (2011) J Clin Invest , vol.121 , pp. 726-738
    • Igaz, L.M.1    Kwong, L.K.2    Lee, E.B.3    Chen-Plotkin, A.4    Swanson, E.5    Unger, T.6    Malunda, J.7
  • 31
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME: Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 1998, 95: 55-66. 10.1016/S0092-8674(00)81782-1
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 32
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S: Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004, 431: 805-810. 10.1038/nature02998
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 33
    • 66749167799 scopus 로고    scopus 로고
    • Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity
    • Subramaniam S, Sixt KM, Barrow R, Snyder SH: Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity. Science 2009, 324: 1327-1330. 10.1126/science.1172871
    • (2009) Science , vol.324 , pp. 1327-1330
    • Subramaniam, S.1    Sixt, K.M.2    Barrow, R.3    Snyder, S.H.4
  • 34
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao RV, Bredesen DE: Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr Opin Cell Biol 2004, 16: 653-662. 10.1016/j.ceb.2004.09.012
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 35
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR: Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000, 10: 524-530. 10.1016/S0962-8924(00)01852-3
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 36
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the mammalian unfolded protein response
    • Harding HP, Calfon M, Urano F, Novoa I, Ron D: Transcriptional and translational control in the mammalian unfolded protein response. Annu Rev Cell Dev Biol 2002, 18: 575-599. 10.1146/annurev.cellbio.18.011402.160624
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 37
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: coping with stress
    • Rutkowski DT, Kaufman RJ: A trip to the ER: coping with stress. Trends Cell Biol 2004, 14: 20-28. 10.1016/j.tcb.2003.11.001
    • (2004) Trends Cell Biol , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 38
    • 0035190132 scopus 로고    scopus 로고
    • Endoplasmic reticulum dysfunction-a common denominator for cell injury in acute and degenerative diseases of the brain?
    • Paschen W, Frandsen A: Endoplasmic reticulum dysfunction-a common denominator for cell injury in acute and degenerative diseases of the brain? J Neurochem 2001, 79: 719-725.
    • (2001) J Neurochem , vol.79 , pp. 719-725
    • Paschen, W.1    Frandsen, A.2
  • 39
    • 77954653461 scopus 로고    scopus 로고
    • Neurotoxic effects of TDP-43 overexpression in C. elegans
    • Ash PE, Zhang YJ, Roberts CM, Saldi T, Hutter H, et al.: Neurotoxic effects of TDP-43 overexpression in C. elegans. Hum Mol Genet 2010, 19: 3206-3218. 10.1093/hmg/ddq230
    • (2010) Hum Mol Genet , vol.19 , pp. 3206-3218
    • Ash, P.E.1    Zhang, Y.J.2    Roberts, C.M.3    Saldi, T.4    Hutter, H.5
  • 40
    • 34250721648 scopus 로고    scopus 로고
    • Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion
    • Hilpert K, Winkler DF, Hancock RE: Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion. Nat Protoc 2007, 2: 1333-1349. 10.1038/nprot.2007.160
    • (2007) Nat Protoc , vol.2 , pp. 1333-1349
    • Hilpert, K.1    Winkler, D.F.2    Hancock, R.E.3
  • 41
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: delivery of a biologically active protein into the mouse
    • Schwarze SR, Ho A, Vocero-Akbani A, Dowdy SF: In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 1999, 285: 1569-1572. 10.1126/science.285.5433.1569
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4


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