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Volumn 24, Issue 6, 2015, Pages 1513-1527

Nuclear TDP-43 causes neuronal toxicity by escaping from the inhibitory regulation by hnRNPs

Author keywords

[No Author keywords available]

Indexed keywords

HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN U; TAR DNA BINDING PROTEIN; DNA BINDING PROTEIN; HNRNP A2; NUCLEAR PROTEIN; POLDIP3 PROTEIN, HUMAN; RNA BINDING PROTEIN; TDP-43 PROTEIN, HUMAN;

EID: 84936070824     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddu563     Document Type: Article
Times cited : (32)

References (50)
  • 1
    • 80755163102 scopus 로고    scopus 로고
    • Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis
    • Ferraiuolo, L., Kirby, J., Grierson, A.J., Sendtner, M. and Shaw, P.J. (2011) Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis. Nat. Rev. Neurol., 7, 616-630.
    • (2011) Nat. Rev. Neurol , vol.7 , pp. 616-630
    • Ferraiuolo, L.1    Kirby, J.2    Grierson, A.J.3    Sendtner, M.4    Shaw, P.J.5
  • 2
    • 84893649256 scopus 로고    scopus 로고
    • State of play in amyotrophic lateral sclerosis genetics
    • Renton, A.E., Chiò, A. and Traynor, B.J. (2014) State of play in amyotrophic lateral sclerosis genetics. Nat. Neurosci., 17, 17-23.
    • (2014) Nat. Neurosci , vol.17 , pp. 17-23
    • Renton, A.E.1    Chiò, A.2    Traynor, B.J.3
  • 3
    • 84864981763 scopus 로고    scopus 로고
    • Advances in understanding the molecular basis of frontotemporal dementia
    • Rademakers, R., Neumann, M. and Mackenzie, I.R. (2012) Advances in understanding the molecular basis of frontotemporal dementia. Nat. Rev. Neurol., 8, 423-434.
    • (2012) Nat. Rev. Neurol , vol.8 , pp. 423-434
    • Rademakers, R.1    Neumann, M.2    Mackenzie, I.R.3
  • 6
    • 84884777626 scopus 로고    scopus 로고
    • Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders
    • Janssens, J. and Van Broeckhoven, C. (2013) Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders. Hum. Mol. Genet., 22, 77-87.
    • (2013) Hum. Mol. Genet , vol.22 , pp. 77-87
    • Janssens, J.1    Van Broeckhoven, C.2
  • 7
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis
    • Ling, S.C., Polymenidou, M. and Cleveland, D.W. (2013) Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron, 79, 416-438.
    • (2013) Neuron , vol.79 , pp. 416-438
    • Ling, S.C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 8
    • 77957317483 scopus 로고    scopus 로고
    • The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation
    • Buratti, E. and Baralle, F.E. (2010) The multiple roles of TDP-43 in pre-mRNA processing and gene expression regulation. RNA Biol., 7, 420-429.
    • (2010) RNA Biol , vol.7 , pp. 420-429
    • Buratti, E.1    Baralle, F.E.2
  • 10
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee, E.B., Lee, V.M. and Trojanowski, J.Q. (2011) Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat. Rev. Neurosci., 13, 38-50.
    • (2011) Nat. Rev. Neurosci , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 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?. Mol. Neurodegener., 7, 27.
    • (2012) Mol. Neurodegener , vol.7 , pp. 27
    • Xu, Z.S.1
  • 12
    • 84855515796 scopus 로고    scopus 로고
    • Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor κB-mediated pathogenic pathways
    • Swarup, V., Phaneuf, D., Dupré, N., Petri, S., Strong, M., Kriz, J. and Julien, J.P. (2011) Deregulation of TDP-43 in amyotrophic lateral sclerosis triggers nuclear factor κB-mediated pathogenic pathways. J. Exp. Med., 208, 2429-2447.
    • (2011) J. Exp. Med , vol.208 , pp. 2429-2447
    • Swarup, V.1    Phaneuf, D.2    Dupré, N.3    Petri, S.4    Strong, M.5    Kriz, J.6    Julien, J.P.7
  • 16
    • 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, G.E., Siddique, T., Zhu, L.J., Lin, S., Greco, K. and Bigio, E.H. (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    Lin, S.6    Greco, K.7    Bigio, E.H.8
  • 17
    • 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
  • 18
    • 84885358733 scopus 로고    scopus 로고
    • Disease animal models of TDP-43 proteinopathy and their pre-clinical applications
    • Liu, Y.C., Chiang, P.M. and Tsai, K.J. (2013) Disease animal models of TDP-43 proteinopathy and their pre-clinical applications. Int. J. Mol. Sci., 14, 20079-20111.
    • (2013) Int. J. Mol. Sci , vol.14 , pp. 20079-20111
    • Liu, Y.C.1    Chiang, P.M.2    Tsai, K.J.3
  • 19
    • 84896532327 scopus 로고    scopus 로고
    • Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life
    • Austin, J.A., Wright, G.S., Watanabe, S., Grossmann, J.G., Antonyuk, S.V., Yamanaka, K. and Hasnain, S.S. (2014) Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life. Proc. Natl Acad. Sci. USA., 111, 4309-4314.
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 4309-4314
    • Austin, J.A.1    Wright, G.S.2    Watanabe, S.3    Grossmann, J.G.4    Antonyuk, S.V.5    Yamanaka, K.6    Hasnain, S.S.7
  • 20
    • 84873314938 scopus 로고    scopus 로고
    • Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins
    • Watanabe, S., Kaneko, K. and Yamanaka, K. (2013) Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins. J. Biol. Chem., 288, 3641-3654.
    • (2013) J. Biol. Chem , vol.288 , pp. 3641-3654
    • Watanabe, S.1    Kaneko, K.2    Yamanaka, K.3
  • 22
    • 79953855830 scopus 로고    scopus 로고
    • TDP-43-induced death is associated with altered regulation of BIM and BclxL and attenuated by caspase-mediated TDP-43 cleavage
    • Suzuki, H., Lee, K. and Matsuoka, M. (2011) TDP-43-induced death is associated with altered regulation of BIM and BclxL and attenuated by caspase-mediated TDP-43 cleavage. J. Biol. Chem., 286, 13171-13183.
    • (2011) J. Biol. Chem , vol.286 , pp. 13171-13183
    • Suzuki, H.1    Lee, K.2    Matsuoka, M.3
  • 23
    • 84855889048 scopus 로고    scopus 로고
    • TDP-43 toxicity is mediated by the unfolded protein response-unrelated induction of C/EBP homologous protein expression
    • Suzuki, H. and Matsuoka, M. (2012) TDP-43 toxicity is mediated by the unfolded protein response-unrelated induction of C/EBP homologous protein expression. J. Neurosci. Res., 90, 641-647.
    • (2012) J. Neurosci. Res , vol.90 , pp. 641-647
    • Suzuki, H.1    Matsuoka, M.2
  • 24
    • 84870474925 scopus 로고    scopus 로고
    • The JNK/c-Jun signaling axis contributes to the TDP-43-induced cell death
    • Suzuki, H. and Matsuoka, M. (2013) The JNK/c-Jun signaling axis contributes to the TDP-43-induced cell death. Mol. Cell Biochem., 372, 241-248.
    • (2013) Mol. Cell Biochem , vol.372 , pp. 241-248
    • Suzuki, H.1    Matsuoka, M.2
  • 25
    • 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, M.J., Igaz, L.M., Wong, M.M., Kwong, L.K., Trojanowski, J.Q. and Lee, V.M. (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    Lee, V.M.6
  • 26
    • 0030221192 scopus 로고    scopus 로고
    • Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids
    • Makkerh, J.P., Dingwall, C. and Laskey, R.A. (1996) Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids. Curr. Biol., 6, 1025-1027.
    • (1996) Curr. Biol , vol.6 , pp. 1025-1027
    • Makkerh, J.P.1    Dingwall, C.2    Laskey, R.A.3
  • 27
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • Kuo, P.H., Doudeva, L.G., Wang, Y.T., Shen, C.K. and Yuan, H.S. (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
  • 28
    • 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
  • 30
    • 77956687928 scopus 로고    scopus 로고
    • Functional diversity of the hnRNPs: past, present and perspectives
    • Han, S.P., Tang, Y.H. and Smith, R. (2010) Functional diversity of the hnRNPs: past, present and perspectives. Biochem. J., 430, 379-392.
    • (2010) Biochem. J , vol.430 , pp. 379-392
    • Han, S.P.1    Tang, Y.H.2    Smith, R.3
  • 32
    • 84859361694 scopus 로고    scopus 로고
    • TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR
    • Fiesel, F.C., Weber, S.S., Supper, J., Zell, A. and Kahle, P.J. (2012) TDP-43 regulates global translational yield by splicing of exon junction complex component SKAR. Nucleic Acids Res., 40, 2668-2682.
    • (2012) Nucleic Acids Res , vol.40 , pp. 2668-2682
    • Fiesel, F.C.1    Weber, S.S.2    Supper, J.3    Zell, A.4    Kahle, P.J.5
  • 33
    • 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, Y.M. and Baralle, F.E. (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    Baralle, F.E.6
  • 40
    • 84893669366 scopus 로고    scopus 로고
    • TDP-43-mediated neurodegeneration: towards a loss-of-function hypothesis?
    • Vanden Broeck, L., Callaerts, P. and Dermaut, B. (2014) TDP-43-mediated neurodegeneration: towards a loss-of-function hypothesis?. Trends Mol. Med., 20, 66-71.
    • (2014) Trends Mol. Med , vol.20 , pp. 66-71
    • Vanden Broeck, L.1    Callaerts, P.2    Dermaut, B.3
  • 44
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum, B.D., Chitta, R.K., High, A.A. and Taylor, J.P. (2010) Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. J. Proteome Res., 9, 1104-1120.
    • (2010) J. Proteome Res , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 45
    • 84901988674 scopus 로고    scopus 로고
    • Abnormal distribution of heterogeneous nuclear ribonucleoproteins in sporadic inclusion body myositis
    • Pinkus, J.L., Amato, A.A., Taylor, J.P. and Greenberg, S.A. (2014) Abnormal distribution of heterogeneous nuclear ribonucleoproteins in sporadic inclusion body myositis. Neuromuscul. Disord., 24, 611-616.
    • (2014) Neuromuscul. Disord , vol.24 , pp. 611-616
    • Pinkus, J.L.1    Amato, A.A.2    Taylor, J.P.3    Greenberg, S.A.4
  • 50
    • 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, F.E., Akiyama, H. and Hasegawa, M. (2009) Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett., 583, 394-400.
    • (2009) FEBS Lett , vol.583 , pp. 394-400
    • Nonaka, T.1    Arai, T.2    Buratti, E.3    Baralle, F.E.4    Akiyama, H.5    Hasegawa, M.6


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