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Volumn 23, Issue 25, 2014, Pages 6863-6877

An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; DNA BINDING PROTEIN; PROTEIN TDP-43;

EID: 84929126317     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddu409     Document Type: Article
Times cited : (52)

References (64)
  • 1
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: conformational diversity and consequences
    • Toyama, B.H. and Weissman, J.S. (2011) Amyloid structure: conformational diversity and consequences. Annu. Rev. Biochem., 80, 557–585.
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 2
    • 84883446343 scopus 로고    scopus 로고
    • Stress granules in neurodegeneration—lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma
    • Bentmann, E., Haass, C. and Dormann, D. (2013) Stress granules in neurodegeneration—lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma. FEBS J., 280, 4348–4370.
    • (2013) FEBS J , vol.280 , pp. 4348-4370
    • Bentmann, E.1    Haass, C.2    Dormann, D.3
  • 3
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee, E.B., Lee, V.M.Y. and Trojanowski, J.Q. (2012) Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat. Rev. Neurosci., 13, 38–50.
    • (2012) Nat. Rev. Neurosci , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.Y.2    Trojanowski, J.Q.3
  • 4
    • 79960040173 scopus 로고    scopus 로고
    • An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
    • Guo, W., Chen, Y., Zhou, X., Kar, A., Ray, P., Chen, X., Rao, E.J., Yang, M., Ye, H., Zhu, L. et al. (2011) An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity. Nat. Struct. Mol. Biol., 18, 822 – 830.
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 822-830
    • Guo, W.1    Chen, Y.2    Zhou, X.3    Kar, A.4    Ray, P.5    Chen, X.6    Rao, E.J.7    Yang, M.8    Ye, H.9    Zhu, L.10
  • 5
    • 34447096691 scopus 로고    scopus 로고
    • Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration
    • Cairns, N., Bigio, E., Mackenzie, I.A., Neumann, M., Lee, V.Y., Hatanpaa, K., White, C. III, Schneider, J., Grinberg, L., Halliday, G. et al. (2007) Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol., 114, 5–22.
    • (2007) Acta Neuropathol , vol.114 , pp. 5-22
    • Cairns, N.1    Bigio, E.2    Mackenzie, I.A.3    Neumann, M.4    Lee, V.Y.5    Hatanpaa, K.6    White, C.7    Schneider, J.8    Grinberg, L.9    Halliday, G.10
  • 6
    • 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.J. 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.J.4    Yuan, H.S.5
  • 10
    • 84878162335 scopus 로고    scopus 로고
    • Drosophila answers to TDP-43 proteinopathies
    • Romano, M., Feiguin, F. and Buratti, E. (2012) Drosophila answers to TDP-43 proteinopathies. J. Amino Acids, 2012, 13.
    • (2012) J. Amino Acids , vol.2012 , pp. 13
    • Romano, M.1    Feiguin, F.2    Buratti, E.3
  • 14
    • 82955235712 scopus 로고    scopus 로고
    • Different clinical and neuropathologic phenotypes of familial ALS with A315E TARDBP mutation
    • Fujita, Y., Ikeda, M., Yanagisawa, T., Senoo, Y. and Okamoto, K. (2011) Different clinical and neuropathologic phenotypes of familial ALS with A315E TARDBP mutation. Neurology, 77, 1427–1431.
    • (2011) Neurology , vol.77 , pp. 1427-1431
    • Fujita, Y.1    Ikeda, M.2    Yanagisawa, T.3    Senoo, Y.4    Okamoto, K.5
  • 19
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Ab amyloid protofibrils by atomic force microscopy
    • Harper, J.D., Wong, S.S., Lieber, C.M. and Lansbury, P.T. Jr (1997) Observation of metastable Ab amyloid protofibrils by atomic force microscopy. Chem. Biol., 4, 119–125.
    • (1997) Chem. Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 20
    • 67651241140 scopus 로고    scopus 로고
    • Circular dichroism techniques: biomolecular and nanostructural analyses—a review
    • Ranjbar, B. and Gill, P. (2009) Circular dichroism techniques: biomolecular and nanostructural analyses—a review. Chem. Biol. Drug Des., 74, 101 – 120.
    • (2009) Chem. Biol. Drug Des , vol.74 , pp. 101-120
    • Ranjbar, B.1    Gill, P.2
  • 21
    • 0037302324 scopus 로고    scopus 로고
    • Structural composition of bI- and bII-proteins
    • Sreerama, N. and Woody, R.W. (2003) Structural composition of bI- and bII-proteins. Protein Sci., 12, 384–388.
    • (2003) Protein Sci , vol.12 , pp. 384-388
    • Sreerama, N.1    Woody, R.W.2
  • 22
    • 1642463952 scopus 로고    scopus 로고
    • Superactivity and conformational changes on alpha-chymotrypsin upon interfacial binding to cationic micelles
    • Celej, M.S., D’Andrea, M.G., Campana, P.T., Fidelio, G.D. and Bianconi, M.L. (2004) Superactivity and conformational changes on alpha-chymotrypsin upon interfacial binding to cationic micelles. Biochem. J., 378, 1059 – 1066.
    • (2004) Biochem. J , vol.378 , pp. 1059-1066
    • Celej, M.S.1    D’Andrea, M.G.2    Campana, P.T.3    Fidelio, G.D.4    Bianconi, M.L.5
  • 23
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen, Y.H., Yang, J.T. and Martinez, H.M. (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry, 11, 4120–4131.
    • (1972) Biochemistry , vol.11 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2    Martinez, H.M.3
  • 24
    • 72149119691 scopus 로고    scopus 로고
    • Fourier transform infrared (FTIR) spectroscopy
    • Berthomieu, C. and Hienerwadel, R. (2009) Fourier transform infrared (FTIR) spectroscopy. Photosynth. Res., 101, 157–170.
    • (2009) Photosynth. Res , vol.101 , pp. 157-170
    • Berthomieu, C.1    Hienerwadel, R.2
  • 25
    • 0343532738 scopus 로고
    • Infrared spectra of polypeptides in various conformations—amide I and II bands
    • Miyazawa, T. and Blout, E.R. (1961) Infrared spectra of polypeptides in various conformations—amide I and II bands. J. Am. Chem. Soc., 83, 712–719.
    • (1961) J. Am. Chem. Soc , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 26
    • 0026101636 scopus 로고
    • Aggregation and secondary structure of synthetic amyloid bA4 peptides of Alzheimer’s disease
    • Hilbich, C., Kisters-Woike, B., Reed, J., Masters, C.L. and Beyreuther, K. (1991) Aggregation and secondary structure of synthetic amyloid bA4 peptides of Alzheimer’s disease. J. Mol. Biol., 218, 149–163.
    • (1991) J. Mol. Biol , vol.218 , pp. 149-163
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyreuther, K.5
  • 27
    • 0033616779 scopus 로고    scopus 로고
    • Interactionsofamyloidb-peptide(1–40) with ganglioside-containing membranes
    • andHorikiri,C
    • Matsuzaki,K.andHorikiri,C.(1999)Interactionsofamyloidb-peptide(1–40) with ganglioside-containing membranes. Biochemistry, 38, 4137–4142.
    • (1999) Biochemistry , vol.38 , pp. 4137-4142
    • Matsuzaki, K1
  • 30
    • 0021368680 scopus 로고
    • Neurofibrillary axonal swellings and amyotrophic lateral sclerosis
    • Delisle, M. and Carpenter, S. (1984) Neurofibrillary axonal swellings and amyotrophic lateral sclerosis. J. Neurol. Sci., 63, 241–250.
    • (1984) J. Neurol. Sci , vol.63 , pp. 241-250
    • Delisle, M.1    Carpenter, S.2
  • 31
    • 0023638714 scopus 로고
    • The pathophysiology of proximal neurofilamentous giant axonal swellings: implications for the pathogenesis of amyotrophic lateral sclerosis
    • Gold, B.G. (1987) The pathophysiology of proximal neurofilamentous giant axonal swellings: implications for the pathogenesis of amyotrophic lateral sclerosis. Toxicology, 46, 125 – 139.
    • (1987) Toxicology , vol.46 , pp. 125-139
    • Gold, B.G.1
  • 32
    • 84880217322 scopus 로고    scopus 로고
    • Expression of ALS-linked TDP-43 mutant in astrocytes causes non-cell-autonomous motor neuron death in rats
    • Tong, J., Huang, C., Bi, F., Wu, Q., Huang, B., Liu, X., Li, F., Zhou, H. and Xia, X.-G. (2013) Expression of ALS-linked TDP-43 mutant in astrocytes causes non-cell-autonomous motor neuron death in rats. EMBO J., 32, 1917–1926.
    • (2013) EMBO J , vol.32 , pp. 1917-1926
    • Tong, J.1    Huang, C.2    Bi, F.3    Wu, Q.4    Huang, B.5    Liu, X.6    Li, F.7    Zhou, H.8    Xia, X.-G.9
  • 33
    • 84919456167 scopus 로고    scopus 로고
    • AxonQuant: a microfluidic chamber culture-coupled algorithm that allows high-throughput quantification of axonal damage
    • Li, Y., Yang, M., Huang, Z., Chen, X., Maloney, M.T., Zhu, L., Liu, J., Yang, Y., Du, S., Jiang, X. et al. (2014) AxonQuant: a microfluidic chamber culture-coupled algorithm that allows high-throughput quantification of axonal damage. Neurosignals, 22, 14 – 29.
    • (2014) Neurosignals , vol.22 , pp. 14-29
    • Li, Y.1    Yang, M.2    Huang, Z.3    Chen, X.4    Maloney, M.T.5    Zhu, L.6    Liu, J.7    Yang, Y.8    Du, S.9    Jiang, X.10
  • 34
    • 77957782470 scopus 로고    scopus 로고
    • Biology of amyloid: structure, function, and regulation
    • Greenwald, J. and Riek, R. (2010) Biology of amyloid: structure, function, and regulation. Structure, 18, 1244–1260.
    • (2010) Structure , vol.18 , pp. 1244-1260
    • Greenwald, J.1    Riek, R.2
  • 35
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D. and Jucker, M. (2012) The amyloid state of proteins in human diseases. Cell, 148, 1188 – 1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 40
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • Tycko, R. (2011) Solid-state NMR studies of amyloid fibril structure. Annu. Rev. Phys. Chem., 62, 279 – 299.
    • (2011) Annu. Rev. Phys. Chem , vol.62 , pp. 279-299
    • Tycko, R.1
  • 43
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer’s b-amyloid fibrils
    • Petkova, A.T., Yau, W.-M. and Tycko, R. (2005) Experimental constraints on quaternary structure in Alzheimer’s b-amyloid fibrils. Biochemistry, 45, 498–512.
    • (2005) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.-M.2    Tycko, R.3
  • 44
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer’s b-amyloid fibrils
    • Paravastu, A.K., Leapman, R.D., Yau, W.-M. and Tycko, R. (2008) Molecular structural basis for polymorphism in Alzheimer’s b-amyloid fibrils. Proc. Natl. Acad. Sci. USA, 105, 18349–18354.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.-M.3    Tycko, R.4
  • 46
    • 20744442130 scopus 로고    scopus 로고
    • A precipitating role for truncated a-synuclein and the proteasome in a-synuclein aggregation: implications for pathogenesis of Parkinson disease
    • Liu, C.-W., Giasson, B.I., Lewis, K.A., Lee, V.M., DeMartino, G.N. and Thomas, P.J. (2005) A precipitating role for truncated a-synuclein and the proteasome in a-synuclein aggregation: implications for pathogenesis of Parkinson disease. J. Biol. Chem., 280, 22670–22678.
    • (2005) J. Biol. Chem , vol.280 , pp. 22670-22678
    • Liu, C.-W.1    Giasson, B.I.2    Lewis, K.A.3    Lee, V.M.4    DeMartino, G.N.5    Thomas, P.J.6
  • 48
    • 70349295278 scopus 로고    scopus 로고
    • Structure–neurotoxicity relationships of amyloid b-protein oligomers
    • Ono, K., Condron, M.M. and Teplow, D.B. (2009) Structure–neurotoxicity relationships of amyloid b-protein oligomers. Proc. Natl. Acad. Sci. USA, 106, 14745–14750.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14745-14750
    • Ono, K.1    Condron, M.M.2    Teplow, D.B.3
  • 49
    • 84865336939 scopus 로고    scopus 로고
    • Cross-seeding effects of amyloid b-protein and a-synuclein
    • Ono, K., Takahashi, R., Ikeda, T. and Yamada, M. (2012) Cross-seeding effects of amyloid b-protein and a-synuclein. J. Neurochem., 122, 883 – 890.
    • (2012) J. Neurochem , vol.122 , pp. 883-890
    • Ono, K.1    Takahashi, R.2    Ikeda, T.3    Yamada, M.4
  • 50
    • 84870916853 scopus 로고    scopus 로고
    • Characterization of b-domains in C-terminal fragments of TDP-43 by scanning tunneling microscopy
    • Xu, M., Zhu, L., Liu, J., Yang, Y., Wu, J.Y. and Wang, C. (2013) Characterization of b-domains in C-terminal fragments of TDP-43 by scanning tunneling microscopy. J. Struct. Biol., 181, 11–16.
    • (2013) J. Struct. Biol , vol.181 , pp. 11-16
    • Xu, M.1    Zhu, L.2    Liu, J.3    Yang, Y.4    Wu, J.Y.5    Wang, C.6
  • 51
    • 84880073331 scopus 로고    scopus 로고
    • Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion
    • Jiang, L.-L., Che, M.-X., Zhao, J., Zhou, C.-J., Xie, M.-Y., Li, H.-Y., He, J.-H. and Hu, H.-Y. (2013) Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion. J. Biol. Chem., 288, 19614–19624.
    • (2013) J. Biol. Chem , vol.288 , pp. 19614-19624
    • Jiang, L.-L.1    Che, M.-X.2    Zhao, J.3    Zhou, C.-J.4    Xie, M.-Y.5    Li, H.-Y.6    He, J.-H.7    Hu, H.-Y.8
  • 54
    • 84878224074 scopus 로고    scopus 로고
    • Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43)
    • Shodai, A., Morimura, T., Ido, A., Uchida, T., Ayaki, T., Takahashi, R., Kitazawa, S., Suzuki, S., Shirouzu, M., Kigawa, T. et al. (2013) Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43). J. Biol. Chem., 288, 14886–14905.
    • (2013) J. Biol. Chem , vol.288 , pp. 14886-14905
    • Shodai, A.1    Morimura, T.2    Ido, A.3    Uchida, T.4    Ayaki, T.5    Takahashi, R.6    Kitazawa, S.7    Suzuki, S.8    Shirouzu, M.9    Kigawa, T.10
  • 55
    • 84878873344 scopus 로고    scopus 로고
    • Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid
    • Bigio, E., Wu, J., Deng, H.-X., Bit-Ivan, E., Mao, Q., Ganti, R., Peterson, M., Siddique, N., Geula, C., Siddique, T. et al. (2013) Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid. Acta Neuropathol., 125, 463 – 465.
    • (2013) Acta Neuropathol , vol.125 , pp. 463-465
    • Bigio, E.1    Wu, J.2    Deng, H.-X.3    Bit-Ivan, E.4    Mao, Q.5    Ganti, R.6    Peterson, M.7    Siddique, N.8    Geula, C.9    Siddique, T.10
  • 56
    • 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. and 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
  • 58
    • 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, 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
  • 61
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR, 6, 277–293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 63
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A.T. (2007) Version 1.2 of the crystallography and NMR system. Nat. Protoc., 2, 2728–2733.
    • (2007) Nat. Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 64
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • 29–32
    • Koradi, R., Billeter, M. and Wuthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph., 14, 51–55, 29–32.
    • (1996) J. Mol. Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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