Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila
Abstract
Tauopathies, including Alzheimer's disease and fronto-temporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), are a group of neurodegenerative disorders characterized by the presence of intraneuronal filamentous inclusions of aberrantly phosphorylated-tau. Tau is a neuronal microtubule-associated protein involved in microtubule assembly and stabilization. Currently, the molecular mechanisms underlying tau-mediated cellular toxicity remain elusive. To address the determinants of tau neurotoxicity, we first characterized the cellular alterations resulting from the over-expression of a mutant form of human tau associated with FTDP-17 (tau V337M) in Drosophila. We found that the over-expression of tau V337M, in Drosophila larval motor neurons, induced disruption of the microtubular network at presynaptic nerve terminals and changes in neuromuscular junctions morphological features. Secondly, we performed a misexpression screen to identify genetic modifiers of the tau V337M-mediated rough eye phenotype. The screening of 1250 mutant Drosophila lines allowed us to identify several components of the cytoskeleton, and particularly from the actin network, as specific modifiers of tau V337M-induced neurodegeneration. Furthermore, we found that numerous tau modulators identified in our screen were involved in the maintenance of synaptic function. Taken together, these findings suggest that disruption of the microtubule network in presynaptic nerve terminals could constitute early events in the pathological process leading to synaptic dysfunction in tau V337M pathology.
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Inhibition or genetic reduction of GSK-3β ameliorates tau-related deficits.
“many investigators have shown that either inhibition or genetic reduction of GSK-3β ameliorates tau-related deficits (94–99).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [98]
The References (ref. 13) list a study reporting that GSK-3β inhibition reverses axonal-transport defects and behavioural phenotypes in Drosophila, supporting the inhibition part of the claim. But this paper’s Discussion (p. 565–566) says its screen did not identify GSK-3β modifiers; it does not report that genetic reduction of GSK-3β ameliorates tau-related deficits. (LLM, conf=0.78)
Experimental — accuracy not yet measuredHere we report novel modifiers distinct from those identified in two recent reports that also screened for genetic modifiers of tau-induced neurodegeneration in Drosophila.
“Here we report novel modifiers distinct from those identified in two recent reports that also screened for genetic modifiers of tau-induced neurodegeneration in Drosophila (52,98).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [98]
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Cites
Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510 · see citing works
Tau is a candidate gene for chromosome 17 frontotemporal dementia
Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374 · see citing works
Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17
Hong, M. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,003 · see citing works
Tauopathy in <i>Drosophila</i> : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · see citing works
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 735 · see citing works
Expanded Polyglutamine Protein Forms Nuclear Inclusions and Causes Neural Degeneration in Drosophila
Warrick, J. M., Paulson, H. L., Gladys L Gray-Board, Bui, Q. T., Fischbeck, K. H., Pittman, R. N., & Bonini, N. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81200-3 · Cited by 669 · see citing works
Identification of genes that modify ataxin-1-induced neurodegeneration
Fernandez-Funez, P., Nino-Rosales, M. L., de Gouyon, B., She, W.-C., Luchak, J. M., Martinez, P., Turiegano, E., Benito, J., Capovilla, M., Skinner, P. J., et al. (2000) · Nature · doi:10.1038/35040584 · Cited by 661 · see citing works
Tau phosphorylation in neuronal cell function and dysfunction
Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624 · see citing works
Genetic Suppression of Polyglutamine Toxicity in Drosophila
Kazemi‐Esfarjani, P., & Benzer, S. (2000) · Science · doi:10.1126/science.287.5459.1837 · Cited by 562 · see citing works
The many faces of filamin: A versatile molecular scaffold for cell motility and signalling
Feng, Y., & Walsh, C. A. (2004) · Nature Cell Biology · doi:10.1038/ncb1104-1034 · Cited by 506 · see citing works
Tau proteins with FTDP‐17 mutations have a reduced ability to promote microtubule assembly
Hasegawa, M., Smith, M. J., & Goedert, M. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01217-4 · Cited by 482 · see citing works
Functional cooperation between the microtubule and actin cytoskeletons
Goode, B. L., Drubin, D. G., & Barnes, G. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)00058-7 · Cited by 475 · see citing works
CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival
Shimura, H., Schwartz, D., Gygi, S. P., & Kosik, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305838200 · Cited by 469 · see citing works
Chaperones increase association of tau protein with microtubules
Dou, F., Netzer, W. J., Tanemura, K., Li, F., Hartl, F. U., Takashima, A., Gouras, G. K., Greengard, P., & Xu, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242720499 · Cited by 462 · see citing works
Axon Pruning during Drosophila Metamorphosis
Watts, R. J., Hoopfer, E. D., & Luo, L. (2003) · Neuron · doi:10.1016/s0896-6273(03)00295-2 · Cited by 376 · see citing works
Direct interaction of microtubule- and actin-based transport motors
Huang, J., Brady, S. T., Richards, B. W., Stenoien, D. L., Resau, J. H., Copeland, N. G., & Jenkins, N. A. (1999) · Nature · doi:10.1038/16722 · Cited by 334 · see citing works
Androgen-Dependent Neurodegeneration by Polyglutamine-Expanded Human Androgen Receptor in Drosophila
Takeyama, K.-I., Ito, S., Yamamoto, A., Tanimoto, H., Furutani, T., Kanuka, H., Miura, M., Tabata, T., & Kato, S. (2002) · Neuron · doi:10.1016/s0896-6273(02)00875-9 · Cited by 300 · see citing works
Accelerated filament formation from tau protein with specific FTDP‐17 missense mutations
Nacharaju, P., Lewis, J. M., Easson, C., Yen, S. H., Hackett, J., Hutton, M., & Yen, S.-H. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00294-x · Cited by 283 · see citing works
GSK-3β inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila
Mudher, A., Shepherd, D., Newman, T. A., Mildren, P., Jukes, J. P., Squire, A., Mears, A., Berg, S., MacKay, D., Asuni, A. A., et al. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001483 · Cited by 265 · see citing works
Effects of frontotemporal dementia FTDP‐17 mutations on heparin‐induced assembly of tau filaments
Goedert, M., Jakes, R., & Crowther, R. A. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00508-6 · Cited by 260 · see citing works
Genetic modifiers of tauopathy in Drosophila
Shulman, J. M., & Feany, M. B. (2003) · Genetics · doi:10.1093/genetics/165.3.1233 · Cited by 256 · see citing works
Neurodegeneration with Tau Accumulation in a Transgenic Mouse Expressing V337M Human Tau
Tanemura, K., Murayama, M., Akagi, T., Hashikawa, T., Tominaga, T., Ichikawa, M., Yamaguchi, H., & Takashima, A. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-01-00133.2002 · Cited by 243 · see citing works
A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis
Osterweil, E. K., Wells, D. G., & Mooseker, M. S. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200410091 · Cited by 226 · see citing works
Dayanandan, R., van Slegtenhorst, M., Mack, T. G. A., Ko, L., Yen, S. H., Leroy, K., Brion, J., Anderton, B. H., Hutton, M. L., & Lovestone, S. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00222-7 · Cited by 210 · see citing works
Shimura, H., Miura-Shimura, Y., & Kosik, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400351200 · Cited by 194 · see citing works
Trojanowski, J. Q., & LEE, V. M. ‐. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05561.x · Cited by 184 · see citing works
Bridgman, P. C. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.1045 · Cited by 151 · see citing works
An unconventional myosin heavy chain gene from Drosophila melanogaster.
Kellerman, K. A., & Miller, K. G. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.4.823 · Cited by 146 · see citing works
Chamberlain, L. H., & Burgoyne, R. D. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741781.x · Cited by 141 · see citing works
T-cell reactivity to multiple myelin antigens in multiple sclerosis patients and healthy controls
Hellings, N., Bar�e, M., Verhoeven, C., D'hooghe, M. B., Medaer, R., Bernard, C. C. A., Raus, J., & Stinissen, P. (2001) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20010201)63:3 · Cited by 138 · see citing works
Gamblin, T. C., King, M. E., Dawson, H. N., Vitek, M. P., Kuret, J., Berry, R. W., & Binder, L. I. (2000) · Biochemistry · doi:10.1021/bi000201f · Cited by 137 · see citing works
Chee, F. C., Mudher, A. K., Cuttle, M. F., Newman, T. A., Mackay, D., Lovestone, S., & Shepherd, D. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.05.029 · Cited by 119 · see citing works
Neural Dysfunction and Neurodegeneration inDrosophilaNa+/K+ATPase Alpha Subunit Mutants
Palladino, M. J., Bower, J. E., Kreber, R. A., & Ganetzky, B. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-04-01276.2003 · Cited by 111 · see citing works
Herreros, L., Rodríguez‐Fernández, J. L., Brown, M. C., Alonso-Lebrero, J. L., Cabañas, C., Sánchez‐Madrid, F., Longo, N., Turner, C. E., & Sánchez‐Mateos, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003970200 · Cited by 109 · see citing works
Zinsmaier, K. E., & Bronk, P. (2001) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00648-7 · Cited by 85 · see citing works
Suzuki, T., Usuda, N., Murata, S., Nakazawa, A., Ohtsuka, K., & Takagi, H. (1999) · Brain Research · doi:10.1016/s0006-8993(98)01083-x · Cited by 82 · see citing works
Chen, G., Turano, B., Ruest, P. J., Hagel, M., Settleman, J. E., & Thomas, S. Μ. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.3.979-987.2005 · Cited by 66 · see citing works
Chattopadhyay, B., Ghosh, S., Gangopadhyay, P. K., Das, S. K., Roy, T., Sinha, K. K., Jha, D. K., Mukherjee, S. C., Chakraborty, A., Singhal, B. S., et al. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00436-1 · Cited by 64 · see citing works
The Multiple Functions of Cysteine-String Protein Analyzed atDrosophilaNerve Terminals
Bronk, P., Nie, Z., Klose, M. K., Dawson-Scully, K. D., Zhang, J., Robertson, R. M., Atwood, H. L., & Zinsmaier, K. E. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3610-04.2005 · Cited by 59 · see citing works
Chau, K. W.-K., Chan, W. Y., Shaw, P. C., & Chan, H. Y. E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.112 · Cited by 33 · see citing works
Depaz, I. M. B., Heras, R. D. L., Kroon, P. A., & Wilce, P. A. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20563 · Cited by 25 · see citing works
In vivo modification of Na+,K+-ATPase activity in Drosophila
Sun, B., Xu, P., Wang, W., & Salvaterra, P. M. (2001) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(01)00470-5 · Cited by 25 · see citing works
Blard, O., Frébourg, T., Campion, D., & Lecourtois, M. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21006 · Cited by 24 · see citing works
Self-citationModulation of oxidative stress resistance in drosophila melanogaster by gene overexpression
Monnier, V., Girardot, F., Chéret, C., Andrés, O., & Tricoire, H. (2002) · genesis · doi:10.1002/gene.10130 · Cited by 18 · see citing works
Heras, R. D. L., Depaz, I. M. B., Jaquet, V., Kroon, P. A., & Wilce, P. A. (2006) · Brain Research · doi:10.1016/j.brainres.2006.10.017 · Cited by 11 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Pandey, U. B., & Nichols, C. D. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.003293 · Cited by 1,155 · see citing works
Tau promotes neurodegeneration through global chromatin relaxation
Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works
“Flies were collected in fresh vials on the day of eclosion and were transferred without anesthesia to fresh vials on days 3, 5, 7, and 9.”
InfluentialBiochemistry of Tau in Alzheimer’s disease and related neurological disorders
Sergeant, N., Bretteville, A., Hamdane, M., Caillet-Boudin, M.-L., Grognet, P., Bombois, S., Blum, D., Delacourte, A., Pasquier, F., Vanmechelen, E., et al. (2008) · Expert Review of Proteomics · doi:10.1586/14789450.5.2.207 · Cited by 300 · see citing works
Tumbarello, D. A., Waxse, B. J., Arden, S. D., Bright, N. A., Kendrick-Jones, J., & Buss, F. (2012) · Nature Cell Biology · doi:10.1038/ncb2589 · Cited by 301 · see citing works
Frandemiche, M. L., De Seranno, S., Rush, T., Borel, E., Elie, A., Arnal, I., Lanté, F., & Buisson, A. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.4261-13.2014 · Cited by 272 · see citing works
Drosophila melanogaster as a model organism for Alzheimer’s disease
Prüßing, K., Voigt, A., & Schulz, J. B. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-35 · Cited by 271 · see citing works
Drosophila melanogaster in the Study of Human Neurodegeneration
Hirth, F. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791556104 · Cited by 236 · see citing works
Myosin motors at neuronal synapses: drivers of membrane transport and actin dynamics
Kneussel, M., & Wagner, W. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3445 · Cited by 191 · see citing works
Neurodegeneration and microtubule dynamics: death by a thousand cuts
Dubey, J., Ratnakaran, N., & Koushika, S. P. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00343 · Cited by 183 · see citing works
BIN1 favors the spreading of Tau via extracellular vesicles
Crotti, A., Sait, H. R., McAvoy, K. M., Estrada, K., Ergun, A., Szak, S., Marsh, G., Jandreski, L., Peterson, M., Reynolds, T. L., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45676-0 · Cited by 171 · see citing works
UBA1: At the Crossroads of Ubiquitin Homeostasis and Neurodegeneration
Groen, E. J. N., & Gillingwater, T. H. (2015) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2015.08.003 · Cited by 157 · see citing works
Chatterjee, S., Sang, T.-K., Lawless, G. M., & Jackson, G. R. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddn326 · Cited by 178 · see citing works
Lin, C., Tsai, P.-I., Wu, R., & Chien, C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1737-10.2010 · Cited by 169 · see citing works
Shulman, J. M., Imboywa, S., Giagtzoglou, N., Powers, M. P., Hu, Y., Devenport, D., Chipendo, P., Chibnik, L. B., Diamond, A., Perrimon, N., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt478 · Cited by 167 · see citing works
Iijima-Ando, K., Sekiya, M., Maruko-Otake, A., Ohtake, Y., Suzuki, E., Lu, B., & Iijima, K. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002918 · Cited by 142 · see citing works
Alzheimer's disease: insights from Drosophila melanogaster models
Moloney, A. M., Sattelle, D. B., Lomas, D. A., & Crowther, D. C. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.11.004 · Cited by 133 · see citing works
Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113 · see citing works
“LOF alleles of VCP/ter94 in Drosophila suppress polyglutamine toxicity (298) and retinal degeneration (299), similar to our finding of LOF of smid suppressing tau toxicity.”
BackgroundInfluentialTransgenic Drosophila models of Alzheimer’s disease and tauopathies
Iijima‐Ando, K., & Iijima, K. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0234-4 · Cited by 110 · see citing works
From tau phosphorylation to tau aggregation: what about neuronal death?
Buée, L., Troquier, L., Burnouf, S., Bélarbi, K., der Jeugd, A. V., Ahmed, T., Fernández-Gómez, F.-J., Caillierez, R., Grosjean, M., Bégard, S., et al. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380967 · Cited by 99 · see citing works
Drosophila as a screening tool to study human neurodegenerative diseases
Lenz, S., Karsten, P., Schulz, J. B., & Voigt, A. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12446 · Cited by 95 · see citing works
Uncoupling neuronal death and dysfunction in Drosophila models of neurodegenerative disease
Chouhan, A. K., Guo, C., Hsieh, Y., Ye, H., Şentürk, M., Zuo, Z., Li, Y., Chatterjee, S., Botas, J., Jackson, G. R., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0333-4 · Cited by 90 · see citing works
HDAC6 mutations rescue human tau-induced microtubule defects in Drosophila
Xiong, Y., Zhao, K., Wu, J., Xu, Z., Jin, S., & Zhang, Y. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207586110 · Cited by 88 · see citing works
Dujardin, S., Colin, M., & Buée, L. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12200 · Cited by 88 · see citing works
Feuillette, S., Miguel, L., Frébourg, T., Campion, D., & Lecourtois, M. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06663.x · Cited by 81 · see citing works
Self-citationFunctional Screening of Alzheimer Pathology Genome-wide Association Signals in Drosophila
Shulman, J. M., Chipendo, P. I., Chibnik, L. B., Aubin, C., Tran, D., Keenan, B. T., Kramer, P. L., Schneider, J. A., Bennett, D., Feany, M. Β., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.01.006 · Cited by 77 · see citing works
Modeling the complex pathology of Alzheimer's disease in Drosophila
Fernandez-Funez, P., de Mena, L., & Rincon-Limas, D. E. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.013 · Cited by 69 · see citing works
Saman, S., Lee, N. C. Y., Inoyo, I. E., Jin, J., Li, Z., Doyle, T., McKee, A. C., & Hall, G. F. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132135 · Cited by 69 · see citing works
Drosophila Models of Alzheimer's Disease: Advances, Limits, and Perspectives
Bouleau, S., & Tricoire, H. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142802 · Cited by 69 · see citing works
Sir2 mediates apoptosis through JNK-dependent pathways in Drosophila
Griswold, A. J., Chang, K. T., Runko, A. P., Knight, M. A., & Min, K. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803837105 · Cited by 66 · see citing works
DnaJA1 Antagonizes Constitutive Hsp70-Mediated Stabilization of Tau
Abisambra, J. F., Jinwal, U. K., Suntharalingam, A., Arulselvam, K., Brady, S., Cockman, M. E., Jin, Y., Zhang, B., & Dickey, C. A. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.02.003 · Cited by 65 · see citing works
Drosophila Models of Tauopathies: What Have We Learned?
Gistelinck, M., Lambert, J., Callaerts, P., Dermaut, B., & Dourlen, P. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/970980 · Cited by 58 · see citing works
Behind the curtain of tauopathy: a show of multiple players orchestrating tau toxicity
Huang, Y., Wu, Z., & Zhou, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2042-8 · Cited by 58 · see citing works
Allen, M., Wang, X., Serie, D., Strickland, S. L., Burgess, J. D., Koga, S., Younkin, C. S., Nguyen, T., Malphrus, K. G., Lincoln, S., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1900-5 · Cited by 58 · see citing works
Liu, Q. F., Lee, J. H., Kim, Y., Lee, S., Hong, Y. K., Hwang, S., Oh, Y., Lee, K., Yun, H. S., Lee, I., et al. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00459 · Cited by 57 · see citing works
Implicating Calpain in Tau-Mediated Toxicity In Vivo
Reinecke, J. B., DeVos, S. L., McGrath, J. P., Shepard, A. M., Goncharoff, D. K., Tait, D. N., Fleming, S. R., Vincent, M. P., & Steinhilb, M. L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023865 · Cited by 52 · see citing works
Benhelli‐Mokrani, H., Mansuroglu, Z., Chauderlier, A., Albaud, B., Gentien, D., Sommer, S., Schirmer, C., Laqueuvre, L. M., Josse, T., Buée, L., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky929 · Cited by 52 · see citing works
Drosophila Models of Proteinopathies: the Little Fly that Could
Rincón-Limas, D. E., Jensen, K., & Fernández-Fúnez, P. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315894 · Cited by 51 · see citing works
Bin1 directly remodels actin dynamics through its BAR domain
Dräger, N. M., Nachman, E., Winterhoff, M., Brühmann, S., Shah, P., Katsinelos, T., Boulant, S., Teleman, A. A., Faix, J., & Jahn, T. R. (2017) · The EMBO Reports · doi:10.15252/embr.201744137 · Cited by 51 · see citing works
Neurogenesis and cell cycle‐reactivated neuronal death during pathogenic tau aggregation
Schindowski, K., Bélarbi, K., Bretteville, A., Ando, K., & Buée, L. (2008) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00377.x · Cited by 50 · see citing works
Alzheimer’s Disease-Related Protein Expression in the Retina of Octodon degus
Du, L. Y., Chang, L., Ardiles, Á. O., Tapia‐Rojas, C., Araya, J., Inestrosa, N. C., Palacios, A. G., & Acosta, M. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135499 · Cited by 47 · see citing works
Integrated analysis of the aging brain transcriptome and proteome in tauopathy
Mangleburg, C. G., Wu, T., Yalamanchili, H. K., Guo, C., Hsieh, Y.-C., Duong, D. M., Dammer, E. B., De Jager, P. L., Seyfried, N. T., Liu, Z., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00405-4 · Cited by 75 · see citing works
Testosterone Is a Strong Correlate of Ghrelin Levels in Men and Postmenopausal Women
Greenman, Y., Rouach, V., Limor, R., Gilad, S., & Stern, N. (2008) · Neuroendocrinology · doi:10.1159/000151768 · Cited by 42 · see citing works
Ubhi, K. K., Shaibah, H., Newman, T. A., Shepherd, D., & Mudher, A. K. (2007) · Invertebrate Neuroscience · doi:10.1007/s10158-007-0052-4 · Cited by 39 · see citing works
Hannan, S. B., Dräger, N. M., Rasse, T. M., Voigt, A., & Jahn, T. R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13532 · Cited by 38 · see citing works
The pivotal role of ubiquitin-activating enzyme E1 (UBA1) in neuronal health and neurodegeneration
Lambert-Smith, I. A., Saunders, D. N., & Yerbury, J. J. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105746 · Cited by 37 · see citing works
Cytotoxic Effects of Environmental Toxins on Human Glial Cells
D‘Mello, F., Braidy, N., Marçal, H., Guillemin, G. J., Rossi, F., Chinian, M., Laurent, D., Teo, C., & Neilan, B. A. (2016) · Neurotoxicity Research · doi:10.1007/s12640-016-9678-5 · Cited by 36 · see citing works
Biological basis for amyloidogenesis in Alzheimer’S disease
Андреева, Т. В., Lukiw, W. J., & Rogaev, E. I. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917020043 · Cited by 36 · see citing works
Evaluation of Traditional Medicines for Neurodegenerative Diseases Using Drosophila Models
Lee, S., Bang, S. M., Lee, J. W., & Cho, K. S. (2014) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2014/967462 · Cited by 36 · see citing works
Chen, X., & Burgoyne, R. D. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-71 · Cited by 32 · see citing works
Recent advances in using Drosophila to model neurodegenerative diseases
Lu, B. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0347-5 · Cited by 31 · see citing works
Feuillette, S., Deramecourt, V., Laquerrière, A., Duyckaerts, C. J., Delisle, M., Maurage, C., Blum, D. L., Buée, L., Frébourg, T., Campion, D., et al. (2010) · Brain Research · doi:10.1016/j.brainres.2010.05.007 · Cited by 31 · see citing works
Self-citationModeling Tauopathy in the Fruit Fly Drosophila melanogaster
Khurana, V. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-15403 · Cited by 31 · see citing works
Giong, H.-K., Subramanian, M., Yu, K., & Lee, J.-S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168465 · Cited by 29 · see citing works
An integrative systems-biology approach defines mechanisms of Alzheimer’s disease neurodegeneration
Leventhal, M. J., Zanella, C. A., Kang, B., Peng, J., Gritsch, D., Liao, Z., Bukhari, H., Wang, T., Pao, P., Danquah, S. A., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59654-w · Cited by 32 · see citing works
NeuroGeM, a knowledgebase of genetic modifiers in neurodegenerative diseases
Na, D., Rouf, M., O’Kane, C. J., Rubinsztein, D. C., & Gsponer, J. A. (2013) · BMC Medical Genomics · doi:10.1186/1755-8794-6-52 · Cited by 26 · see citing works
The Power and Richness of Modelling Tauopathies in Drosophila
Papanikolopoulou, K., & Skoulakis, E. M. C. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8193-1 · Cited by 28 · see citing works
Studying tauopathies in Drosophila: A fruitful model
Sun, M., & Chen, L. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.03.029 · Cited by 27 · see citing works
Hwang, S., Jeong, H., Hong, E., Joo, H. M., Cho, K. S., & Nam, S. Y. (2019) · Biology Open · doi:10.1242/bio.036657 · Cited by 26 · see citing works
Tau Interacting Proteins: Gaining Insight into the Roles of Tau in Health and Disease
Stancu, I., Ferraiolo, M., Terwel, D., & Dewachter, I. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_13 · Cited by 23 · see citing works
Modelling Tauopathies in Drosophila : Insights from the Fruit Fly
Cowan, C. M., Sealey, M. A., Quraishe, S., Targett, M.-T., Marcellus, K. A., Allan, D. W., & Mudher, A. K. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/598157 · Cited by 23 · see citing works
Sinadinos, C., Quraishe, S., Sealey, M. A., Samson, P. B., Mudher, A. K., & Wyttenbach, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121534 · Cited by 22 · see citing works
Chanu, S. I., & Sarkar, S. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9858-6 · Cited by 20 · see citing works
Mical modulates Tau toxicity via cysteine oxidation in vivo
Prifti, E., Tsakiri, E. N., Vourkou, E., Stamatakis, G. M., Samiotaki, M. K., Skoulakis, E. M. C., & Papanikolopoulou, K. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01348-1 · Cited by 19 · see citing works
Simple model systems reveal conserved mechanisms of Alzheimer’s disease and related tauopathies
Jiang, Y., & MacNeil, L. T. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00664-x · Cited by 20 · see citing works
Graham, J. F., Kurian, D., Agarwal, S., Toovey, L., Hunt, L., Kirby, L., Pinheiro, T. J. T., Banner, S. J., & Gill, A. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026813 · Cited by 19 · see citing works
Xiong, Z., Jeon, M., Allaway, R. J., Kang, J., Park, D., Lee, J., Jeon, H., Ko, M., Jiang, H., Zheng, M., et al. (2021) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1009302 · Cited by 18 · see citing works
Beaver, M., Karisetty, B. C., Zhang, H., Bhatnagar, A., Armour, E. M., Parmar, V., Brown, R., Xiang, M., & Elefant, F. (2021) · Epigenetics · doi:10.1080/15592294.2021.1959742 · Cited by 16 · see citing works
Identification of TCERG1 as a new genetic modulator of TDP-43 production in Drosophila
Pons, M., Prieto‐Sánchez, S., Miguel, L., Frébourg, T., Campion, D., Suñé, C., & Lecourtois, M. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0639-5 · Cited by 16 · see citing works
Self-citationDo the Genes of the Innate Immune Response Contribute to Neuroprotection in Drosophila?
Cantera, R., & Barrio, R. (2014) · Journal of Innate Immunity · doi:10.1159/000365195 · Cited by 16 · see citing works
Atoki, A. V., Aja, P. M., Ondari, E. N., & Shinkafi, T. S. (2023) · International Journal of Food Properties · doi:10.1080/10942912.2023.2243050 · Cited by 19 · see citing works
The Drosophila model system to study tau action
Trotter, M., Stephens, T. D., McGrath, J. P., & Steinhilb, M. L. (2017) · Methods in cell biology · doi:10.1016/bs.mcb.2017.06.006 · Cited by 14 · see citing works
UsingDrosophilamodels of neurodegenerative diseases for drug discovery
Newman, T. A., Sinadinos, C., Johnston, A. H., Sealey, M. A., & Mudher, A. K. (2011) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2011.549124 · Cited by 14 · see citing works
A Connected Network of Interacting Proteins Is Involved in Human-Tau Toxicity in Drosophila
Feuillette, S., Charbonnier, C., Frébourg, T., Campion, D., & Lecourtois, M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00068 · Cited by 14 · see citing works
Self-citationThe role of wild-type tau in Alzheimer’s disease and related tauopathies
Lo, C. H., & Sachs, J. N. (2020) · JoLS Journal of Life Sciences · doi:10.36069/jols/20201201 · Cited by 14 · see citing works
Nitta, Y., Kawai, H., Maki, R., Osaka, J., Hakeda‐Suzuki, S., Nagai, Y., Doubková, K., Uehara, T., Watanabe, K., Kosaki, K., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddac307 · Cited by 14 · see citing works
Tau Protein: Function and Pathology
Rosenmann, H., Blum, D. L., Kayed, R., & Ittner, L. M. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/707482 · Cited by 12 · see citing works
Therapeutic Targets in Alzheimer's Disease and Related Tauopathies
Corbo, C. P., & Alonso, A. D. C. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385506-0.00002-8 · Cited by 13 · see citing works
Hsp40s play distinct roles during the initial stages of apolipoprotein B biogenesis
Kumari, D., Fisher, E. A., & Brodsky, J. L. (2021) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-09-0436 · Cited by 11 · see citing works
Untangling the role of tau in Alzheimer’s disease: A unifying hypothesis
Bhatia, N. S., & Hall, G. F. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0114-5 · Cited by 11 · see citing works
The ubiquitin ligase Ariadne-1 regulates neurotransmitter release via ubiquitination of NSF
Ramírez, J., Morales, M., Osinalde, N., Martínez-Padrón, I., Mayor, U., & Ferrús, A. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100408 · Cited by 12 · see citing works
Proteome-Scale Mapping of Perturbed Proteostasis in Living Cells.Preprint
Lam, I., Hallacli, E., & Khurana, V. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034124 · Cited by 8 · see citing works
Direct and Indirect Effects of Filamin A on Tau Pathology in Neuronal Cells
Levert, S., Pilliod, J., Aumont, É., Armanville, S., Tremblay, C., Calon, F., & Leclerc, N. M. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03121-w · Cited by 9 · see citing works
Unraveling the Basis of Neurodegeneration using the Drosophila Eye
Fernández-Fúnez, P., Sanchez-Garcia, J., & Rincón-Limas, D. E. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8232-1_10 · Cited by 9 · see citing works
Yang, P., Liu, H., Li, Y., Gao, Q., Chen, X., Chang, J., Li, Y., Chen, S., Dong, R., Wu, H., et al. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.959832 · Cited by 8 · see citing works
Codon-optimized TDP-43 mediates neurodegeneration in a Drosophila model of ALS/FTLD
Yusuff, T., Chang, Y., Sang, T., Jackson, G. R., & Chatterjee, S. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.881638 · Cited by 7 · see citing works
Mouchel‐Vielh, E., Bloyer, S., Salvaing, J., Randsholt, N. B., & Peronnet, F. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01231.x · Cited by 7 · see citing works
Identification of Tau Toxicity Modifiers in the Drosophila Eye
Dourlen, P. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_26 · Cited by 7 · see citing works
The Biology and Pathobiology of Tau Protein
Hall, G. F. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-788-0_15 · Cited by 6 · see citing works
Khani, M., Nafissi, S., Shamshiri, H., Moazzeni, H., Taheri, H., Sadeghi, M., Salehi, N., Chitsazian, F., & Elahi, E. (2022) · European Journal of Neurology · doi:10.1111/ene.15528 · Cited by 3 · see citing works
Drosophila Models of Tauopathy
Ali, Y., Ruan, K., & Zhai, R. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00054-8 · Cited by 2 · see citing works
Insights into amyloid disease from fly models
Chen, K., & Crowther, D. C. (2014) · Essays in Biochemistry · doi:10.1042/bse0560069 · Cited by 2 · see citing works
Codon-optimized TDP-43-mediated neurodegeneration in a Drosophila model for ALS/FTLDPreprint
Yusuff, T., Chatterjee, S., Chang, Y., Sang, T., & Jackson, G. R. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/696963 · Cited by 2 · see citing works
MeDUsA: A novel system for automated axon quantification to evaluate neuroaxonal degenerationPreprint
Nitta, Y., Kawai, H., Osaka, J., Hakeda‐Suzuki, S., Nagai, Y., Doubková, K., Suzuki, T., Tavosanis, G., & Sugie, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.25.465674 · Cited by 2 · see citing works
Prefoldin 5 is a microtubule-associated protein that suppresses Tau aggregation and neurotoxicityPreprint
Bisht, A., Pippadpally, S., Majumder, S., Gopi, A. T., Das, A., Sahi, C., Ramaswami, M., & Kumar, V. (2024) · eLife · doi:10.7554/elife.104691.3 · Cited by 4 · see citing works
Sergeant, N., & Buée, L. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-6787-9_4 · Cited by 1 · see citing works
Neurodegeneration models in Drosophila
Roy, B., & Jackson, G. R. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511920585.012 · Cited by 1 · see citing works
Experimental Models of Tau Aggregation
Buck, K., Jahn, T. R., & Gasparini, L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811353-0.00070-1 · Cited by 1 · see citing works
Tau, Tangles and Tauopathies: Insights from Drosophila Disease Models
Nisha, N., Pragati, Tandon, S., Aqsa, A., Aggarwal, P., & Sarkar, S. (2019) · Springer eBooks · doi:10.1007/978-981-13-2218-1_8 · Cited by 1 · see citing works
Towards individualized medicine: flies lead the way
Elliott, J. L., & Yin, J. C. P. (2007) · Future Neurology · doi:10.2217/14796708.2.4.389 · Cited by 1 · see citing works
- Authors
- Blard, O., Feuillette, S., Bou, J., Chaumette, B., Frébourg, T., Campion, D., & Lecourtois, M.
- Affiliations
- Inserm (FR)
- Corresponding author
- Lecourtois, Magalie
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-02-19
- Volume
- 16
- Issue
- 5
- Pages
- 555-566
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2112207786
- Cited by
- 110
- References
- 45
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 4 · 2022: 5 · 2021: 7 · 2020: 6 · 2019: 6 · 2018: 4 · 2017: 3 · 2016: 6 · 2015: 8 · 2014: 9 · 2013: 9 · 2012: 8
- FWCI
- 4.25
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Sanofi
- Région Normandie
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurobiology and Insect Physiology Research
- Keywords
- tauopathy, FTDP-17, cytoskeleton, actin networks, presynaptic terminals, neuromuscular junction, synaptic dysfunction, genetic modifiers, rough eye phenotype, Alzheimer's disease
- MeSH terms
- Animals, Cytoskeletal Proteins, Cytoskeleton, Drosophila melanogaster, Eye, Female, Humans, Larva, Male, Methionine, Nerve Degeneration, Neuromuscular Junction, Peptides, Phenotype, Phosphorylation, Valine, tau Proteins, Molecular Chaperones, Mutant Proteins
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