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Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo
Open accessAbstract
Mitochondrial abnormalities have been documented in Alzheimer's disease and related neurodegenerative disorders, but the causal relationship between mitochondrial changes and neurodegeneration, and the specific mechanisms promoting mitochondrial dysfunction, are unclear. Here, we find that expression of human tau results in elongation of mitochondria in both Drosophila and mouse neurons. Elongation is accompanied by mitochondrial dysfunction and cell cycle-mediated cell death, which can be rescued in vivo by genetically restoring the proper balance of mitochondrial fission and fusion. We have previously demonstrated that stabilization of actin by tau is critical for neurotoxicity of the protein. Here, we demonstrate a conserved role for actin and myosin in regulating mitochondrial fission and show that excess actin stabilization inhibits association of the fission protein DRP1 with mitochondria, leading to mitochondrial elongation and subsequent neurotoxicity. Our results thus identify actin-mediated disruption of mitochondrial dynamics as a direct mechanism of tau toxicity in neurons in vivo.
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“Pathologic tau causes an increase in actin stabilization18 that inhibits association of the fission protein Drp1 with mitochondria, leading to mitochondrial elongation and the production of reactive oxygen species44.”
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“No statistical methods were used to predetermine sample sizes but our sample sizes are similar to those reported in previous publications 7,16,44.”
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
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
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601
Lee, T., & Luo, L. (1999) · Neuron · doi:10.1016/s0896-6273(00)80701-1 · Cited by 2,540
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Prevalence of Dementia in the United States: The Aging, Demographics, and Memory Study
Plassman, B. L., Langa, K. M., Fisher, G. G., Heeringa, S. G., Weir, D. R., Ofstedal, M. B., Burke, J. R., Hurd, M. D., Potter, G. G., Rodgers, W. L., et al. (2007) · Neuroepidemiology · doi:10.1159/000109998 · Cited by 1,932
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Mitochondrial proteins as biomarkers of cellular senescence and age-associated diseases
Panfilova, A. S., Zubareva, T., Mironova, E. S., Mazzoccoli, G., Marasco, M. G. P., Balazovskaia, S., Yablonsky, P., & Kvetnoy, I. M. (2025) · Aging · doi:10.18632/aging.206305 · Cited by 8
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Nithianandam, V., Sarkar, S., & Feany, M. Β. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae018 · Cited by 6
Self-citationDietary Alterations in Impaired Mitochondrial Dynamics Due to Neurodegeneration
Ashraf, G. M., Chatzichronis, S., Alexiou, A. T., Firdousi, G., Kamal, M. A., & Ganash, M. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.893018 · Cited by 6
Impairment of Mitochondrial Dynamics: A Target For the Treatment of Neurological Disorders?
Su, Y.-C., & Qi, X. (2013) · Future Neurology · doi:10.2217/fnl.13.8 · Cited by 5
When two worlds collide: actin dynamics on endomembranes regulates membrane trafficking
Marchan, M. F., & Bear, J. E. (2025) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2025.102596 · Cited by 4
Mohl, G. A., Dixon, G., Marzette, E., McKetney, J., Samelson, A. J., Serras, C. P., Jin, J., Ariqat, N., Keys, A., Chavira, C., et al. (2026) · npj Dementia · doi:10.1038/s44400-026-00076-w · Cited by 4
Genetic modifiers of synucleinopathies—lessons from experimental models
Lee, R. M. Q., & Koh, T. (2023) · Oxford Open Neuroscience · doi:10.1093/oons/kvad001 · Cited by 4
Huang, Y. Q., Ma, C., Zhu, L., Kong, L., Huang, C., Yang, W., He, J., Yang, M., Huang, L., Yuan, L., et al. (2024) · Environmental Toxicology · doi:10.1002/tox.24444 · Cited by 4
Role of Tau Protein Hyperphosphorylation in Diabetic Retinal Neurodegeneration
Mu, J., Zhang, Z., Jiang, C., Geng, H., & Duan, J. (2025) · Journal of Ophthalmology · doi:10.1155/joph/3278794 · Cited by 5
Regulation of mitochondrial structure by the actin cytoskeleton
Wu, Y., Ren, X., Shi, P., & Wu, C. (2023) · Cytoskeleton · doi:10.1002/cm.21804 · Cited by 4
Kelliny, S., Xiong, J., Bobrovskaya, L., & Zhou, X. (2021) · Neurotoxicity Research · doi:10.1007/s12640-021-00405-2 · Cited by 4
Sun, W., Li, X., Chu, Z., Huang, T., & Wu, W. (2021) · Central European Journal of Immunology · doi:10.5114/ceji.2021.111444 · Cited by 3
Schmauck‐Medina, T., Patrick-Brown, T. D. J. H., Zhang, S., Gilbert, A., & Fang, E. F. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-89906-2.00007-1 · Cited by 3
Lee, D.-S., Kim, T. H., Park, H., & Kim, J.-E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065875 · Cited by 3
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Beckmann, A., Ramirez, P., Gamez-Guijarro, M., Ray, W. J., & Frost, B. E. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.05.434166 · Cited by 3
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Lei, C., Zhang, B., Yamaguchi, J., Tamura, R., Cao, X., Liu, Y., Seki, M., Suzuki, Y., Suzuki, K., Tanida, I., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.12.622892 · Cited by 3
Kim, J.-E., Wang, S. H., & Kang, T. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110586 · Cited by 2
Mahadik, N., Paruchuri, S. N., Arif, R., Coutts, A. S., Barron, G. A., Lin, P. K. T., Chatterjee, S., & Thompson, C. J. (2025) · Scientific Reports · doi:10.1038/s41598-025-22924-0 · Cited by 2
Liang, S., Zhu, Y., Su, J., Luo, C., & Yang, C. (2026) · Drug Development Research · doi:10.1002/ddr.70224 · Cited by 2
Peng, Y., Wang, S.-S., Lai, K.-D., Ye, J.-R., He, W.-B., Yan, X., Zhang, Z., Chu, S.-F., & Chen, N. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-025-01709-1 · Cited by 4
Yang, G., Xu, X., & Xu, Y. (2026) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2026.112057 · Cited by 2
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Ali, Y., Ruan, K., & Zhai, R. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00054-8 · Cited by 2
Re-energising the brain: glucose metabolism, Tau protein and memory in ageing and dementia
Robbins, M. (2024) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2023.57 · Cited by 3
Alzheimer’s Disease—Molecular Defect, Public Perceptions and Stigma in South Africa
Maduna, T., & Loos, B. (2021) · Springer eBooks · doi:10.1007/978-981-16-2546-6_4 · Cited by 4
Khandia, R., Pandey, M. K., Garg, R. K., Khan, A. A., Baklanov, I. S., Alanazi, A. M., Nepali, P., Gurjar, P., & Choudhary, O. P. (2024) · Annals of Medicine and Surgery · doi:10.1097/ms9.0000000000001725 · Cited by 2
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Perbet, R., Zufferey, V., Leroux, É., Parietti, E., Espourteille, J., Culebras, L., Perriot, S., du Pasquier, R., Bégard, S., Deramecourt, V., et al. (2023) · bioRxiv · doi:10.1101/2023.02.15.527595
Hou, X., Richardson, T., Heckman, M. G., Fiesel, F. C., White, L. J., Koga, S., Ross, O. A., Dickson, D. W., & Springer, W. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02964-6 · Cited by 2
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Norambuena, A., Wallrabe, H. K., Cao, R., Wang, D. B., Silva, A., Švindrych, Z., Periasamy, A., Hu, S., Kim, D. Y., Tanzi, R. E., et al. (2018) · SSRN Electronic Journal · doi:10.2139/ssrn.3188445 · Cited by 1
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Guha, S. K., Cheng, A., Carroll, T., King, D. P., Koren, S. A., Swords, S., Nehrke, K. W., & Johnson, G. V. W. (2021) · Research Square · doi:10.21203/rs.3.rs-1096882/v1
Kelliny, S., Xiong, J., Bobrovskaya, L., & Zhou, X. (2021) · Research Square · doi:10.21203/rs.3.rs-306628/v1
Nairn, A. C., & Leslie, S. N. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.734280180.793553827
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Li, X., Wu, P., Bao, D., Guo, Z., Jiang, H., Sui, Y., Bian, W., Wang, S., Zhang, F., Wu, J., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4254091/v1
Tang, Z., Guo, M., Ding, Y., Wen, Y., Li, B., Xiao, Y., Ni, R., Guan, Z.-Z., & Qi, X. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.24.625068 · Cited by 1
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Goncalves, A. (2020) · theses.fr (ABES) · doi:10.70675/b42db6dez88a0z4a14z93eez8f51d19d46f5
de Noiron, J. (2021) · theses.fr (ABES) · doi:10.70675/493e3435ze4f9z40afza15bz7c5f951985f5
Denéchaud, M. (2022) · theses.fr (ABES) · doi:10.70675/623e7224z0cb0z47b1z8a22z549acf553ac0
Sayehmiri, F., Parvenous, M., Vakili, K. G., Ebrahimi, R., Batool, Z., Bazgir, N., Kazemi, K., Moafi, M., Ebrahimi, M. J., & Hajiesmaeili, M. (2026) · Metabolic Brain Disease · doi:10.1007/s11011-026-01809-9
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Gao, J., Shukla, D., Ding, M., Qin, S., Tang, F., Guerrero, E., Vicuna, L., Xu, J., Li, H., Miyagi, M., et al. (2026) · Nature Aging · doi:10.1038/s43587-026-01166-3
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Metadata
- Authors
- DuBoff, B., Götz, J., & Feany, M. B.
- Affiliations
- Brigham and Women's Hospital (US)
- The University of Queensland (AU)
- ORCID
- Götz, Jürgen
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 75
- Issue
- 4
- Pages
- 618-632
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3428596
- OpenAlex
- W2082970812
- Cited by
- 377
- References
- 75
- Citations by year
- 2026: 15 · 2025: 25 · 2024: 24 · 2023: 30 · 2022: 24 · 2021: 43 · 2020: 26 · 2019: 25 · 2018: 28 · 2017: 30 · 2016: 24 · 2015: 24 · 2014: 29 · 2013: 27 · 2012: 3
- FWCI
- 17.81
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (F31AG032839, R21AG028074, R01AG033518, R01AG019790)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- tau protein, neurodegeneration, Drp1, mitochondrial fission, mitochondrial fusion, mitochondrial dynamics, mitochondrial elongation, actin filament stabilization, myosin, Alzheimer's disease, mitochondrial dysfunction, tau toxicity, Drosophila neurons, mouse neurons
- MeSH terms
- Actins, Analysis of Variance, Animals, Cytoplasm, Cytoskeletal Proteins, Disease Models, Animal, Drosophila, Gene Expression Regulation, Humans, Microtubule-Associated Proteins, Mitochondria, Mutation, Myosins, Nerve Degeneration, Neurons, tau Proteins, Cell Death, Gelsolin, Cell Cycle Proteins, GTP-Binding Proteins, In Situ Nick-End Labeling, GTP Phosphohydrolases, Mitochondrial Proteins, Tauopathies, ATP Synthetase Complexes, Drosophila Proteins, Animals, Genetically Modified, Dynamins, RNA Interference, MicroRNAs, Green Fluorescent Proteins, Voltage-Dependent Anion Channels, Mice
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