The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
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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“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]
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“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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Citations
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
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
Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17.
Hong, M., Zhukareva, V., Vogelsberg-Ragaglia, V., Wszolek, Z., Reed, L., Miller, B., Geschwind, D., Bird, T., McKeel, D., Goate, A., et al. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,024
Tauopathy in Drosophila : 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
CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 723
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
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
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
Genetic Suppression of Polyglutamine Toxicity in Drosophila
Kazemi‐Esfarjani, P., & Benzer, S. (2000) · Science · doi:10.1126/science.287.5459.1837 · Cited by 563
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
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Powis, R. A. (2016) · Edinburgh Research Archive (University of Edinburgh)
The ubiquitin ligase Ariadne-1 regulates NSF for neurotransmitter releasePreprint
Ramírez, J., Morales, M., Osinalde, N., Martínez-Padrón, I., Mayor, U., & Ferrús, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.23.916619
Identification of Tau Toxicity Modifiers in the Drosophila Eye
Dourlen, P. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_27
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.104691.1
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. (2025) · eLife · doi:10.7554/elife.104691.2
Additional file 1 of 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., Jager, P. L. D., Seyfried, N. T., Liu, Z., et al. (2020) · Figshare · doi:10.6084/m9.figshare.13024037
Additional file 1 of Mical modulates Tau toxicity via cysteine oxidation in vivo
Prifti, E., Tsakiri, E. N., Vourkou, E., Stamatakis, G. M., Samiotaki, M., Skoulakis, E. M. C., & Papanikolopoulou, K. (2022) · Figshare · doi:10.6084/m9.figshare.19518576
Etude des fonctions des Sidéroflexines, une nouvelle famille de protéines mitochondriales
Tifoun, N. (2021) · theses.fr (ABES) · doi:10.70675/19d943dcz4ccfz40b3z8e0ez5530fe24e55f
Metadata
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical 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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