Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Open accessAbstract
Alzheimer's disease (AD) is characterized by amyloid-beta (Abeta) and tau deposition in brain. It has emerged that Abeta toxicity is tau dependent, although mechanistically this link remains unclear. Here, we show that tau, known as axonal protein, has a dendritic function in postsynaptic targeting of the Src kinase Fyn, a substrate of which is the NMDA receptor (NR). Missorting of tau in transgenic mice expressing truncated tau (Deltatau) and absence of tau in tau(-/-) mice both disrupt postsynaptic targeting of Fyn. This uncouples NR-mediated excitotoxicity and hence mitigates Abeta toxicity. Deltatau expression and tau deficiency prevent memory deficits and improve survival in Abeta-forming APP23 mice, a model of AD. These deficits are also fully rescued with a peptide that uncouples the Fyn-mediated interaction of NR and PSD-95 in vivo. Our findings suggest that this dendritic role of tau confers Abeta toxicity at the postsynapse with direct implications for pathogenesis and treatment of AD.
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In AD models, absence of tau rescues behavioral impairments and reduces neurotoxicity despite no significant changes in Aβ levels.
“For example, in AD models, the absence of tau has been shown to rescue behavioral impairments and reduce neurotoxicity, despite no significant changes in Aβ levels [75–79].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [77]
In multiple mouse disease models, tau ablation is associated with protective effects.
“Interestingly, in multiple mouse disease models, tau ablation has been associated with protective effects.”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [77]
The literature has established a role for tau in regulating glutamatergic synaptic function, where it interacts with Fyn, NMDARs, PSD-95, and SynGAP1.
“The literature has established a role for tau in regulating glutamatergic synaptic function, where it interacts with Fyn, NMDARs, PSD-95, and SynGAP1 [41, 77, 105].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [77]
Once tau is eliminated, glia appear better able to mount context and disease-appropriate responses, including elimination of toxic species, reduction in kinase activation, and modulation of downstream signaling, potentially explaining the broad protective effects of tau ablation across pathological models.
“Once tau is eliminated, glia appear better able to mount context and disease-appropriate responses, including elimination of toxic species [144], reduction in kinase activation, and modulation of downstream signaling [76, 78, 145], potentially explaining the broad protective effects of tau ablation across pathological models.”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [145]
Growing evidence indicates a critical interplay between Aβ and tau pathologies that drives disease progression, potentially through synapses and glial activation.
“A growing body of evidence highlights the critical interplay between these pathologies, potentially through synapses and glial activation, that drives disease progression.”
From Unique transcriptomic alterations in 5XFAD;PS19 mouse model identify glial lipid dysregulation and coordinated microglial–oligodendrocyte responses (2026) · cites this paper as [6]
Phosphorylation can alter tau subcellular localization to dendritic spines or alter its affinity for the plasma membrane, thereby causing alterations in synaptic function.
“Apart from its effects on microtubule binding, phosphorylation can alter tau subcellular localization to dendritic spines (127) or can alter its affinity for the plasma membrane (128), thereby causing alterations in synaptic function (127,129).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [129]
Across various animal models that exhibit epilepsy, reducing tau levels reduces network hyperexcitability, seizure severity, and latency to seizure stages.
“Across various animal models that exhibit epilepsy, reducing tau levels reduces network hyperexcitability, seizure severity, and latency to seizure stages (Roberson et al., 2007; Ittner et al., 2010; DeVos et al., 2013; Holth et al., 2013; Wang and Mandelkow, 2016; Ali et al., 2019).”
From Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms (2022) · cites this paper as Ittner et al., 2010
Ab oligomers cause tau mislocalization.
“Ab oligomers also cause tau mislocalization (77,78).”
Tau activity, localization and function in synapses appear to be phosphorylation-dependent.
“While little is known about the cellular mechanisms linking Tau with synaptic function, Tau activity, localization and function in synapses appear to be phosphorylation-dependent [58].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [58]
Basal phosphorylation of synaptic NMDARs at Y1472 by fyn is notably reduced in Tau−/− mice.
“leading to basal phosphorylation of synaptic NMDARs at Y1472 by fyn which is notably reduced in Tau−/− mice (Ittner et al., 2010).”
From Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice (2017) · cites this paper as Ittner et al., 2010
Under normal conditions the physical tau/fyn association results in targeting of fyn kinase to postsynaptic sites, leading to basal phosphorylation of synaptic NMDARs at Y1472 by fyn.
“Under normal conditions the physical tau/fyn association results in targeting of fyn kinase to postsynaptic sites (Ittner et al., 2010) leading to basal phosphorylation of synaptic NMDARs at Y1472 by fyn which is notably reduced in Tau−/− mice (Ittner et al., 2010).”
From Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice (2017) · cites this paper as Ittner et al., 2010
In Alzheimer's disease, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments.
“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Ittner et al., 2010
Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules.
“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Ittner et al., 2010
Tau is also present in dendrites and postsynaptic compartments.
“Recent studies demonstrate that tau is also present in dendrites and postsynaptic compartments [128–130].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [128]
Aβ aggregates and hyperphosphorylated tau protein exert a synergistic effect on impairing synapse function.
“Aβ aggregates and hyperphosphorylated tau protein exert synergistic effect on impairing synapse function.91–93”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [92]
Although human tau gene MAPT mutations per se only cause frontotemporal dementia rather than AD, tau mediates Aβ toxicity to promote the pathological process of AD.
“Although the human tau gene MAPT mutations per se only cause frontotemporal dementia (FTD) rather than AD,462 tau mediates Aβ toxicity to promote the pathological process of AD.92,137”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [92]
Some data suggest that Aβ toxicity is partially mediated through tau, as tau knockout mice are protected against Aβ-induced insults including cognitive effects, seizures, survival, axonal transport, and DNA double-stranded breaks.
“Some data suggest that Aβ toxicity is partially mediated through tau (50–52) as the tau knockout mouse has proven to be protected against a growing number of Aβ-induced insults, including those affecting cognition (50, 53), seizures (14, 50, 51, 54, 55), survival (50, 51, 54), axonal transport (52), and double-stranded breaks in DNA (55).”
From Tau reduction prevents neuronal loss and reverses pathological tau deposition and seeding in mice with tauopathy (2017) · cites this paper as [54]
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Self-citationIncreased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model
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Self-citationGSK‐3 in Neurodegenerative Diseases
Lei, P., Ayton, S., Bush, A. I., & Adlard, P. A. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/189246 · Cited by 177 · see citing works
Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160 · see citing works
Dourlen, P., Kilinc, D., Malmanche, N., Chapuis, J., & Lambert, J.-C. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02004-0 · Cited by 168 · see citing works
- Authors
- Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., Eckert, A., Staufenbiel, M., Hardeman, E., & Götz, J.
- Affiliations
- The University of Sydney (AU)
- University of Basel (CH)
- Novartis (Switzerland) (CH)
- UNSW Sydney (AU)
- Corresponding author
- Ittner, Lars M.
- Götz, Jürgen
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-08
- Volume
- 142
- Issue
- 3
- Pages
- 387-397
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2022532556
- Cited by
- 1,821
- References
- 65
- Citations by year
- 2026: 65 · 2025: 103 · 2024: 80 · 2023: 109 · 2022: 110 · 2021: 139 · 2020: 147 · 2019: 117 · 2018: 146 · 2017: 115 · 2016: 118 · 2015: 120 · 2014: 114 · 2013: 108 · 2012: 98
- FWCI
- 73.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1112 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Australian Research Council
- National Health and Medical Research Council
- National Medical Research Council
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, amyloid-beta toxicity, Alzheimer's disease, Fyn, NMDA receptor, excitotoxicity, PSD-95, APP23 transgenic mice, memory impairment, truncated tau
- MeSH terms
- Disks Large Homolog 4 Protein, Alzheimer Disease, Animals, Brain, Dendrites, Humans, Membrane Proteins, Memory Disorders, Mice, Transgenic, Synapses, Receptors, N-Methyl-D-Aspartate, Amyloid beta-Peptides, tau Proteins, Intracellular Signaling Peptides and Proteins, Proto-Oncogene Proteins c-fyn, Mice, Guanylate Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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