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Journal of Amino Acids
Volume 2012 (2012), Article ID 356081, 13 pages
Drosophila Answers to TDP-43 Proteinopathies
1Department of Life Sciences, University of Trieste, Via A. Valerio 28, 34127 Trieste, Italy
2International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34149 Trieste, Italy
Received 5 December 2011; Accepted 23 January 2012
Academic Editor: Yijuang Chern
Copyright © 2012 Maurizio Romano et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- J. Bilen and N. M. Bonini, “Drosophila as a model for human neurodegenerative disease,” Annual Review of Genetics, vol. 39, pp. 153–171, 2005.
- L. T. Reiter, L. Potocki, S. Chien, M. Gribskov, and E. Bier, “A systematic analysis of human disease-associated gene sequences in Drosophila melanogaster,” Genome Research, vol. 11, no. 6, pp. 1114–1125, 2001.
- M. D. W. Piper, D. Skorupa, and L. Partridge, “Diet, metabolism and lifespan in Drosophila,” Experimental Gerontology, vol. 40, no. 11, pp. 857–862, 2005.
- G. M. Rubin, M. D. Yandell, J. R. Wortman et al., “Comparative genomics of the eukaryotes,” Science, vol. 287, no. 5461, pp. 2204–2215, 2000.
- J. M. Shulman, L. M. Shulman, W. J. Weiner, and M. B. Feany, “From fruit fly to bedside: translating lessons from Drosophila models of neurodegenerative disease,” Current Opinion in Neurology, vol. 16, no. 4, pp. 443–449, 2003.
- F. Feiguin, V. K. Godena, G. Romano, A. D'Ambrogio, R. Klima, and F. E. Baralle, “Depletion of TDP-43 affects Drosophila motoneurons terminal synapsis and locomotive behavior,” The FEBS Letters, vol. 583, no. 10, pp. 1586–1592, 2009.
- Y. Lu, J. Ferris, and F. B. Gao, “Frontotemporal dementia and amyotrophic lateral sclerosis-associated disease protein TDP-43 promotes dendritic branching,” Molecular Brain, vol. 2, no. 1, article 30, 2009.
- A. Voigt, D. Herholz, F. C. Fiesel et al., “TDP-43-mediated neuron loss in vivo requires RNA-binding activity,” PLoS ONE, vol. 5, no. 8, Article ID e12247, 2010.
- F. C. Fiesel, A. Voigt, S. S. Weber et al., “Knockdown of transactive response DNA-binding protein (TDP-43) downregulates histone deacetylase 6,” The EMBO Journal, vol. 29, no. 1, pp. 209–221, 2010.
- K. A. Hanson, S. H. Kim, D. A. Wassarman, and R. S. Tibbetts, “Ubiquilin modifies TDP-43 toxicity in a Drosophila model of amyotrophic lateral sclerosis (ALS),” Journal of Biological Chemistry, vol. 285, no. 15, pp. 11068–11072, 2010.
- Y. Li, P. Ray, and E. J. Rao, “A Drosophila model for TDP-43 proteinopathy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 7, pp. 3169–3174, 2010.
- G. P. Ritson, S. K. Custer, B. D. Freibaum et al., “TDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97,” Journal of Neuroscience, vol. 30, no. 22, pp. 7729–7739, 2010.
- P. S. Estes, A. Boehringer, R. Zwick, J. E. Tang, B. Grigsby, and D. C. Zarnescu, “Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS,” Human Molecular Genetics, vol. 20, no. 12, pp. 2308–2321, 2011.
- W. Guo, Y. Chen, X. Zhou et al., “An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity,” Nature Structural & Molecular Biology, vol. 18, no. 7, pp. 822–830, 2011.
- N. A. Lanson Jr., A. Maltare, H. King et al., “A Drosophila model of FUS-related neurodegeneration reveals genetic interaction between FUS and TDP-43,” Human Molecular Genetics, vol. 20, no. 13, pp. 2510–2523, 2011.
- H.-Y. Li, P.-A. Yeh, H.-C. Chiu, C.-Y. Tang, and B. P. Tu, “Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation,” PLoS ONE, vol. 6, no. 8, Article ID e23075, 2011.
- M.-J. Lin, C.-W. Cheng, and C.-K. J. Shen, “Neuronal function and dysfunction of Drosophila dTDP,” PLoS ONE, vol. 6, no. 6, Article ID e20371, 2011.
- L. Miguel, T. Frébourg, D. Campion, and M. Lecourtois, “Both cytoplasmic and nuclear accumulations of the protein are neurotoxic in Drosophila models of TDP-43 proteinopathies,” Neurobiology of Disease, vol. 41, no. 2, pp. 398–406, 2011.
- V. K. Godena, G. Romano, M. Romano et al., “TDP-43 regulates Drosophila neuromuscular junctions growth by modulating futsch/MAP1B levels and synaptic microtubules organization,” PLoS ONE, vol. 6, no. 3, Article ID e17808, 2011.
- F. Rodrigues, I. Schmidt, and C. Klämbt, “Comparing peripheral glial cell differentiation in Drosophila and vertebrates,” Cellular and Molecular Life Sciences, vol. 68, pp. 55–69, 2011.
- I. F. Wang, L. S. Wu, and C. K. J. Shen, “TDP-43: an emerging new player in neurodegenerative diseases,” Trends in Molecular Medicine, vol. 14, no. 11, pp. 479–485, 2008.
- E. Buratti and F. E. Baralle, “Chapter 1 the molecular links between TDP-43 dysfunction and neurodegeneration,” Advances in Genetics, vol. 66, pp. 1–34, 2009.
- H. Seelaar, J. D. Rohrer, Y. A. L. Pijnenburg, N. C. Fox, and J. C. van Swieten, “Clinical, genetic and pathological heterogeneity of frontotemporal dementia: a review,” Journal of Neurology, Neurosurgery and Psychiatry, vol. 82, pp. 476–486, 2011.
- M. J. Strong and W. Yang, “The frontotemporal syndromes of ALS. Clinicopathological correlates,” Journal of Molecular Neuroscience, vol. 45, no. 3, pp. 648–655, 2011.
- M. Neumann, D. M. Sampathu, L. K. Kwong et al., “Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis,” Science, vol. 314, no. 5796, pp. 130–133, 2006.
- T. Arai, M. Hasegawa, H. Akiyama et al., “TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis,” Biochemical and Biophysical Research Communications, vol. 351, no. 3, pp. 602–611, 2006.
- R. H. Baloh, “TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration,” The FEBS Journal, vol. 278, no. 19, pp. 3539–3549, 2011.
- M. Hasegawa, T. Arai, T. Nonaka et al., “Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis,” Annals of Neurology, vol. 64, no. 1, pp. 60–70, 2008.
- Y. Inukai, T. Nonaka, T. Arai et al., “Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS,” The FEBS Letters, vol. 582, no. 19, pp. 2899–2904, 2008.
- T. Arai, I. R. A. Mackenzie, M. Hasegawa et al., “Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies,” Acta Neuropathologica, vol. 117, no. 2, pp. 125–136, 2009.
- L. M. Igaz, L. K. Kwong, A. Chen-Plotkin et al., “Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies,” Journal of Biological Chemistry, vol. 284, no. 13, pp. 8516–8524, 2009.
- F. Kametani, T. Nonaka, T. Suzuki et al., “Identification of casein kinase-1 phosphorylation sites on TDP-43,” Biochemical and Biophysical Research Communications, vol. 382, no. 2, pp. 405–409, 2009.
- M. Neumann, L. K. Kwong, E. B. Lee et al., “Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies,” Acta Neuropathologica, vol. 117, no. 2, pp. 137–149, 2009.
- T. Nonaka, T. Arai, E. Buratti, F. E. Baralle, H. Akiyama, and M. Hasegawa, “Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells,” The FEBS Letters, vol. 583, no. 2, pp. 394–400, 2009.
- E. Buratti and F. E. Baralle, “Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9,” The Journal of Biological Chemistry, vol. 276, pp. 36337–36343, 2001.
- Y. M. Ayala, S. Pantano, A. D'Ambrogio et al., “Human, Drosophila, and C. elegans TDP43: nucleic acid binding properties and splicing regulatory function,” Journal of Molecular Biology, vol. 348, no. 3, pp. 575–588, 2005.
- A. D'Ambrogio, E. Buratti, C. Stuani et al., “Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo,” Nucleic Acids Research, vol. 37, no. 12, pp. 4116–4126, 2009.
- E. Buratti, A. Brindisi, M. Giombi, S. Tisminetzky, Y. M. Ayala, and F. E. Baralle, “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,” Journal of Biological Chemistry, vol. 280, no. 45, pp. 37572–37584, 2005.
- I. Wegorzewska, S. Bell, N. J. Cairns, T. M. Miller, and R. H. Baloh, “TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 44, pp. 18809–18814, 2009.
- T. F. Gendron, K. A. Josephs, and L. Petrucelli, “Review: transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration,” Neuropathology and Applied Neurobiology, vol. 36, no. 2, pp. 97–112, 2010.
- C. Lagier-Tourenne, M. Polymenidou, and D. W. Cleveland, “TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration,” Human Molecular Genetics, vol. 19, no. 1, Article ID ddq137, pp. R46–R64, 2010.
- N. R. Stallings, K. Puttaparthi, C. M. Luther, D. K. Burns, and J. L. Elliott, “Progressive motor weakness in transgenic mice expressing human TDP-43,” Neurobiology of Disease, vol. 40, no. 2, pp. 404–414, 2010.
- H. Zhou, C. Huang, H. Chen et al., “Transgenic rat model of neurodegeneration caused by mutation in the TDP gene,” PLoS Genetics, vol. 6, no. 3, Article ID e1000887, 2010.
- C. C. Weihl, P. Temiz, S. E. Miller et al., “TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia,” Journal of Neurology, Neurosurgery and Psychiatry, vol. 79, no. 10, pp. 1186–1189, 2008.
- C. Cook, Y. J. Zhang, Y. F. Xu, D. W. Dickson, and L. Petrucelli, “TDP-43 in neurodegenerative disorders,” Expert Opinion on Biological Therapy, vol. 8, no. 7, pp. 969–978, 2008.
- A. S. Chen-Plotkin, V. M. Y. Lee, and J. Q. Trojanowski, “TAR DNA-binding protein 43 in neurodegenerative disease,” Nature Reviews Neurology, vol. 6, no. 4, pp. 211–220, 2010.
- C. C. Weihl, A. Pestronk, and V. E. Kimonis, “Valosin-containing protein disease: inclusion body myopathy with Paget's disease of the bone and fronto-temporal dementia,” Neuromuscular Disorders, vol. 19, no. 5, pp. 308–315, 2009.
- M. Badadani, A. Nalbandian, G. D. Watts et al., “VCP associated inclusion body myopathy and paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease,” PLoS ONE, vol. 5, no. 10, Article ID e13183, 2010.
- S. K. Custer, M. Neumann, H. Lu, A. C. Wright, and J. P. Taylor, “Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone,” Human Molecular Genetics, vol. 19, no. 9, Article ID ddq050, pp. 1741–1755, 2010.
- S. C. Ling, C. P. Albuquerque, J. S. Han et al., “ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 30, pp. 13318–13323, 2010.
- I. R. A. Mackenzie, R. Rademakers, and M. Neumann, “TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia,” The Lancet Neurology, vol. 9, no. 10, pp. 995–1007, 2010.
- H. Maruyama, H. Morino, H. Ito et al., “Mutations of optineurin in amyotrophic lateral sclerosis,” Nature, vol. 465, no. 7295, pp. 223–226, 2010.
- J. B. Guinto, G. P. Ritson, P. J. Taylor, and M. S. Forman, “Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy,” Acta Neuropathologica, vol. 114, no. 1, pp. 55–61, 2007.
- T. J. Kwiatkowski, D. A. Bosco, A. L. LeClerc et al., “Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis,” Science, vol. 323, no. 5918, pp. 1205–1208, 2009.
- C. Vance, B. Rogelj, T. Hortobágyi et al., “Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6,” Science, vol. 323, no. 5918, pp. 1208–1211, 2009.
- D. Dormann and C. Haass, “TDP-43 and FUS: a nuclear affair,” Trends in Neurosciences, vol. 34, no. 7, pp. 339–348, 2011.
- H. X. Deng, H. Zhai, E. H. Bigio et al., “FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis,” Annals of Neurology, vol. 67, no. 6, pp. 739–748, 2010.
- B. D. Freibaum, R. K. Chitta, A. A. High, and J. P. Taylor, “Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery,” Journal of Proteome Research, vol. 9, no. 2, pp. 1104–1120, 2010.
- C. F. Sephton, C. Cenik, A. Kucukural et al., “Identification of neuronal RNA targets of TDP-43-containing ribonucleoprotein complexes,” Journal of Biological Chemistry, vol. 286, no. 2, pp. 1204–1215, 2011.
- J.-W. Wang, J. R. Brent, A. Tomlinson, N. A. Shneider, and B. D. McCabe, “The ALS-associated proteins FUS and TDP-43 function together to affect Drosophila locomotion and life span,” Journal of Clinical Investigation, vol. 121, no. 10, pp. 4118–4126, 2011.
- S. H. Kim, N. P. Shanware, M. J. Bowler, and R. S. Tibbetts, “Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA,” Journal of Biological Chemistry, vol. 285, no. 44, pp. 34097–34105, 2010.
- S. H. Kim, Y. Shi, K. A. Hanson et al., “Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1,” Journal of Biological Chemistry, vol. 284, no. 12, pp. 8083–8092, 2009.
- H. S. Ko, T. Uehara, K. Tsuruma, and Y. Nomura, “Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains,” The FEBS Letters, vol. 566, no. 1–3, pp. 110–114, 2004.
- A. L. Mah, G. Perry, M. A. Smith, and M. J. Monteiro, “Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation,” Journal of Cell Biology, vol. 151, no. 4, pp. 847–862, 2000.
- H. Doi, K. Mitsui, M. Kurosawa, Y. MacHida, Y. Kuroiwa, and N. Nukina, “Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates,” The FEBS Letters, vol. 571, no. 1–3, pp. 171–176, 2004.
- U. B. Pandey, Y. Batlevi, E. H. Baehrecke, and J. P. Taylor, “Erratum: HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration,” Autophagy, vol. 3, no. 6, pp. 643–645, 2007.
- U. B. Pandey, Z. Nie, Y. Batlevi et al., “HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS,” Nature, vol. 447, no. 7146, pp. 859–863, 2007.
- G. Du, X. Liu, X. Chen et al., “Drosophila histone deacetylase 6 protects dopaminergic neurons against α-synuclein toxicity by promoting inclusion formation,” Molecular Biology of the Cell, vol. 21, no. 13, pp. 2128–2137, 2010.
- J. Y. Lee, H. Koga, Y. Kawaguchi et al., “HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy,” The EMBO Journal, vol. 29, no. 5, pp. 969–980, 2010.
- T. Hummel, K. Krukkert, J. Roos, G. Davis, and C. Klämbt, “Drosophila Futsch/22C10 is a MAP1B-like protein required for dendritic and axonal development,” Neuron, vol. 26, no. 2, pp. 357–370, 2000.
- P. E. Ash, Y. J. Zhang, C. M. Roberts et al., “Neurotoxic effects of TDP-43 overexpression in C. elegans,” Human Molecular Genetics, vol. 19, no. 16, Article ID ddq230, pp. 3206–3218, 2010.
- A. C. Wilson, B. N. Dugger, D. W. Dickson, and D.-S. Wang, “TDP-43 in aging and Alzheimer's disease—a review,” International Journal of Clinical and Experimental Pathology, vol. 4, no. 2, pp. 147–155, 2011.