Tau proteinopathies and the prion concept
Abstract
The ordered assembly of a small number of proteins into amyloid filaments is central to age-related neurodegenerative diseases. Tau is the most commonly affected of these proteins. In sporadic diseases, assemblies of tau form in a stochastic manner in certain brain regions, from where they appear to spread in a deterministic way, giving rise to disease symptoms. Over the past decade, multiple lines of evidence have shown that assembled tau behaves like a prion. More recently, electron cryo-microscopy of tau filaments has shown that distinct conformers are present in different diseases, with no inter-individual variation for a given disease.
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Short fibrils and oligomers of tau can transfer from one neuron to another and spread pathology throughout the brain in a prion-like manner.
“Over the past several years, it has become increasingly evident that short fibrils and oligomers of tau can transfer from one neuron to another and thereby spread pathology throughout the brain in a prion-like manner (4, 5, 6).”
From MAP2 caps tau fibrils and inhibits aggregation (2023) · cites this paper as [5]
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
Cryo-EM structures of tau filaments from Alzheimer’s disease
Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061 · see citing works
Self-citationTransmission and spreading of tauopathy in transgenic mouse brain
Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · see citing works
Self-citationPropagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works
A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau
Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · see citing works
Propagation of Tau Misfolding from the Outside to the Inside of a Cell
Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · see citing works
Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036 · see citing works
Self-citationSaman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985 · see citing works
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971 · see citing works
Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929 · see citing works
Self-citationHeparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds
Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859 · see citing works
Trans-cellular Propagation of Tau Aggregation by Fibrillar Species
Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552 · see citing works
LRP1 is a master regulator of tau uptake and spread
Rauch, J. N., Luna, G., Guzman, E., Audouard, M., Challis, C., Sibih, Y. E., Leshuk, C., Hernandez, I., Wegmann, S., Hyman, B. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2156-5 · Cited by 541 · see citing works
Biology and Genetics of Prions Causing Neurodegeneration
Prusiner, S. B. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155524 · Cited by 455 · see citing works
MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments
Al-Bassam, J., Ozer, R. S., Safer, D., Halpain, S., & Milligan, R. A. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200201048 · Cited by 327 · see citing works
Usenovic, M., Niroomand, S., Drolet, R. E., Yao, L., Gaspar, R. C., Hatcher, N. G., Schachter, J., Renger, J. J., & Parmentier-Batteur, S. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.1523-15.2015 · Cited by 245 · see citing works
Amyloid accelerates tau propagation and toxicity in a model of early Alzheimer’s disease
Pooler, A. M., Polydoro, M., Maury, E. A., Nicholls, S. B., Reddy, S. M., Wegmann, S., William, C., Saqran, L., Cagsal-Getkin, O., Pitstick, R., et al. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0199-x · Cited by 236 · see citing works
Schmidt, M., Zhukareva, V., Newell, K., Lee, V., & Trojanowski, J. (2001) · Acta Neuropathologica · doi:10.1007/s004010000330 · Cited by 230 · see citing works
Tau Does Not Stabilize Axonal Microtubules but Rather Enables Them to Have Long Labile Domains
Qiang, L., Sun, X., Austin, T. O., Muralidharan, H., Jean, D. C., Liu, M., Yu, W., & Baas, P. W. (2018) · Current Biology · doi:10.1016/j.cub.2018.05.045 · Cited by 222 · see citing works
Cofactors are essential constituents of stable and seeding-active tau fibrils
Fichou, Y., Lin, Y., Rauch, J. N., Vigers, M., Zeng, Z., Srivastava, M., Keller, T. J., Freed, J. H., Kosik, K. S., & Han, S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810058115 · Cited by 128 · see citing works
Using Human iPSC-Derived Neurons to Model TAU Aggregation
Verheyen, A., Diels, A., Dijkmans, J., Oyelami, T., Meneghello, G., Mertens, L., Versweyveld, S., Borgers, M., Buist, A., Peeters, P., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0146127 · Cited by 86 · see citing works
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The <scp>NLRP3</scp> inflammasome modulates tau pathology and neurodegeneration in a tauopathy model
Stancu, I. C., Lodder, C., Botella Lucena, P., Vanherle, S., Gutiérrez de Ravé, M., Terwel, D., Bottelbergs, A., & Dewachter, I. (2022) · Glia · doi:10.1002/glia.24160 · Cited by 72 · see citing works
MAP2 caps tau fibrils and inhibits aggregation
Holden, M. R., Krzesinski, B. J., Weismiller, H. A., Shady, J. R., & Margittai, M. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104891 · Cited by 13 · see citing works
- Authors
- Goedert, M.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Michel Goedert
- ORCID
- Michel Goedert
- Venue
- Progress in Molecular Biology and Translational Science
- Publisher
- Elsevier
- Published
- 2020
- Volume
- 175
- Pages
- 239-259
- ISSN
- 1877-1173 (ISSN-L)
- OpenAlex
- W3084416161
- Cited by
- 38
- References
- 21
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 4 · 2023: 6 · 2022: 10 · 2021: 7
- FWCI
- 23.76
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Progress in molecular biology and translational science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- tau protein, prion-like behavior, neurodegenerative diseases, tau filaments, disease spread
- MeSH terms
- Amino Acid Sequence, Animals, Brain, Humans, Phenotype, Prions, tau Proteins, Neurodegenerative Diseases, Tauopathies
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