Propagation of Tau aggregates
Open accessAbstract
Since 2009, evidence has accumulated to suggest that Tau aggregates form first in a small number of brain cells, from where they propagate to other regions, resulting in neurodegeneration and disease. Propagation of Tau aggregates is often called prion-like, which refers to the capacity of an assembled protein to induce the same abnormal conformation in a protein of the same kind, initiating a self-amplifying cascade. In addition, prion-like encompasses the release of protein aggregates from brain cells and their uptake by neighbouring cells. In mice, the intracerebral injection of Tau inclusions induced the ordered assembly of monomeric Tau, followed by its spreading to distant brain regions. Short fibrils constituted the major species of seed-competent Tau. The existence of several human Tauopathies with distinct fibril morphologies has led to the suggestion that different molecular conformers (or strains) of aggregated Tau exist.
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A synapse-centred hypothesis does not preclude the spreading hypothesis, which could be either a downstream pathological event or a potential trigger of Tau-related excitotoxicity and synaptic failure.
“A synapse-centred hypothesis also does not preclude the spreading hypothesis [34, 66], which could be either a downstream pathological event or a potential trigger of Tau-related excitotoxicity and synaptic failure.”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [34]
The Introduction describes Tau aggregates spreading between cells and resulting in degeneration, and the Conclusion places propagation downstream of Tau assembly. Neither passage establishes how a synapse-centred hypothesis relates to spreading or identifies spreading as a trigger of Tau-related excitotoxicity and synaptic failure. (LLM, conf=0.82)
Experimental — accuracy not yet measuredIn animal models that express tau only in certain brain regions, or that are injected with exogenous tau, spreading of tau pathology to anatomically connected regions occurs over time.
“In animal models that express tau only in certain brain regions, or that are injected with exogenous tau, spreading of tau pathology to anatomically connected regions occurs over time54,64,228.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [64]
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Tau-targeting therapies for Alzheimer disease
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Induction of a transmissible tau pathology by traumatic brain injury
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Tau Isoforms: Gaining Insight into MAPT Alternative Splicing
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Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved
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Current Status of Clinical Trials on Tau Immunotherapies
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Age-related diseases as vicious cycles
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Precisely Defined Conjugated Oligoelectrolytes for Biosensing and Therapeutics
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Tau immunotherapies: Lessons learned, current status and future considerations
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The role of heparan sulfates in protein aggregation and their potential impact on neurodegeneration
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Fate and propagation of endogenously formed Tau aggregates in neuronal cells
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Tau Secretion: Good and Bad for Neurons
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Filamentous Aggregates Are Fragmented by the Proteasome Holoenzyme
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Anti-herpetic tau preserves neurons via the cGAS-STING-TBK1 pathway in Alzheimer’s disease
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Tau misfolding efficiently propagates between individual intact hippocampal neurons
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Hallmarks of neurodegenerative disease: A systems pharmacology perspective
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Potentiating tangle formation reduces acute toxicity of soluble tau species in the rat
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Monoclonal Antibody Therapy in Alzheimer’s Disease
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Zinc Induces Temperature-Dependent Reversible Self-Assembly of Tau
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Therapeutic Potential of Different Natural Products for the Treatment of Alzheimer’s Disease
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14-3-3/Tau Interaction and Tau Amyloidogenesis
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Implication of type 4 NADPH oxidase (NOX4) in tauopathy
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Exploring rare cellular activity in more than one million cells by a transscale scope
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Cytosolic condensates rich in polyserine define subcellular sites of tau aggregation
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EFhd2 Affects Tau Liquid–Liquid Phase Separation
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Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges
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Relevance of host tau in tau seeding and spreading in tauopathies
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In vivo network models identify sex differences in the spread of tau pathology across the brain
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Tau protein aggregation: Key features to improve drug discovery screening
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Transcellular Spreading of Tau in Tauopathies
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Planar cell polarity gene Fuz triggers apoptosis in neurodegenerative disease models
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Selective Detection of Misfolded Tau From Postmortem Alzheimer’s Disease Brains
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Alzheimer’s Disease Genetics: Review of Novel Loci Associated with Disease
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Terminal Capping of an Amyloidogenic Tau Fragment Modulates Its Fibrillation Propensity
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Photodynamic studies reveal rapid formation and appreciable turnover of tau inclusions
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Recent advances in cellular biosensor technology to investigate tau oligomerization
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Clearance of intracellular tau protein from neuronal cells via VAMP8-induced secretion
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Peripheral Pathways to Neurovascular Unit Dysfunction, Cognitive Impairment, and Alzheimer’s Disease
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Is it Useful to Classify PSP and CBD as Different Disorders? Yes
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Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
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Identification of the three zinc-binding sites on tau protein
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Site-Specific Phospho-Tau Aggregation-Based Biomarker Discovery for AD Diagnosis and Differentiation
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Insights into the Structural Conformations of the Tau Protein in Different Aggregation Status
Pinzi, L., Bisi, N., Sorbi, C., Franchini, S., Tonali, N., & Rastelli, G. (2023) · Molecules · doi:10.3390/molecules28114544 · Cited by 20 · see citing works
Preparation and Characterization of Tau Oligomer Strains
Sengupta, U., Murillo, M. C., & Kayed, R. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-7816-8_9 · Cited by 20 · 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
Targeting Prion-like Cis Phosphorylated Tau Pathology in Neurodegenerative Diseases
Albayram, Ö., Angeli, P. A., Bernstein, E. R., Baxley, S., Gao, Z. J., Lu, K. P., & Zhou, X. Z. (2018) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000443 · Cited by 19 · see citing works
Intrinsically disordered proteins (IDPs) studied by EPR and in-cell EPR
Weickert, S., Cattani, J., & Drescher, M. (2018) · Royal Society of Chemistry eBooks · doi:10.1039/9781788013888-00001 · Cited by 18 · see citing works
Alyenbaawi, H., Allison, W. T., & Mok, S. (2020) · Biomolecules · doi:10.3390/biom10111487 · Cited by 18 · see citing works
Somatic Mutations and Alzheimer’s Disease
Downey, J., Lam, J. C. K., Li, V. O. K., & Gozes, I. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-220643 · Cited by 17 · see citing works
Shin, W. S., Di, J., Murray, K. A., Sun, C., Li, B., Bitan, G., & Jiang, L. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00268 · Cited by 17 · see citing works
RetractedUntangling the tauopathies: Current concepts of tau pathology and neurodegeneration
Ling, H. (2017) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2017.07.031 · Cited by 17 · see citing works
Wu, F., Li, W., Lu, H., & Li, L. (2025) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2025.101003 · Cited by 16 · see citing works
- Authors
- Goedert, M., & Spillantini, M. G.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- University of Cambridge (GB)
- Corresponding author
- Goedert, Michel
- Venue
- Molecular Brain
- Published
- 2017-05-30
- Volume
- 10
- Issue
- 1
- Pages
- 18-18
- ISSN
- 1756-6606 (ISSN-L)
- PMC
- PMC5450399
- OpenAlex
- W2617946428
- Cited by
- 213
- References
- 84
- Citations by year
- 2026: 15 · 2025: 17 · 2024: 16 · 2023: 13 · 2022: 24 · 2021: 27 · 2020: 25 · 2019: 42 · 2018: 25 · 2017: 9
- FWCI
- 3.39
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Molecular Brain (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Apollo
- Funders
- National Centre for the Replacement, Refinement and Reduction of Animals in Research (NC/C013102/1)
- 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 aggregates, prion-like propagation, tauopathy, neurodegeneration, fibril morphology, intracerebral injection
- MeSH terms
- Animals, Humans, tau Proteins, Protein Isoforms, Protein Aggregates
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