Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Open accessAbstract
Axonal transport deficits in Alzheimer’s disease (AD) are attributed to amyloid β (Aβ) peptides and pathological forms of the microtubule-associated protein tau. Genetic ablation of tau prevents neuronal overexcitation and axonal transport deficits caused by recombinant Aβ oligomers. Relevance of these findings to naturally secreted Aβ and mechanisms underlying tau’s enabling effect are unknown. Here we demonstrate deficits in anterograde axonal transport of mitochondria in primary neurons from transgenic mice expressing familial AD-linked forms of human amyloid precursor protein. We show that these deficits depend on Aβ1–42 production and are prevented by tau reduction. The copathogenic effect of tau did not depend on its microtubule binding, interactions with Fyn, or potential role in neuronal development. Inhibition of neuronal activity, N-methyl-d-aspartate receptor function, or glycogen synthase kinase 3β (GSK3β) activity or expression also abolished Aβ-induced transport deficits. Tau ablation prevented Aβ-induced GSK3β activation. Thus, tau allows Aβ oligomers to inhibit axonal transport through activation of GSK3β, possibly by facilitating aberrant neuronal activity.
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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 [78]
The Results section reports that tau ablation prevented Aβ-associated axonal transport deficits in cultured neurons without altering Aβ levels in their growth medium. The Introduction also describes prior evidence linking tau to Aβ-induced cell death and behavioral alterations. But this paper does not show that tau absence rescues behavioral impairments or reduces neurotoxicity in AD models; its direct finding concerns axonal transport. (LLM, conf=0.88)
Experimental — accuracy not yet measuredOnce 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 [78]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredIn 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 [78]
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- Authors
- Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L.
- Affiliations
- Gladstone Institutes (US)
- Corresponding author
- Vossel, Keith A.
- Mucke, Lennart
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2015-05-11
- Volume
- 209
- Issue
- 3
- Pages
- 419-433
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC4427789
- OpenAlex
- W2150110395
- Cited by
- 167
- References
- 97
- Citations by year
- 2026: 15 · 2025: 10 · 2024: 16 · 2023: 11 · 2022: 13 · 2021: 14 · 2020: 18 · 2019: 13 · 2018: 15 · 2017: 14 · 2016: 19 · 2015: 9
- FWCI
- 14.00
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute on Aging (K23AG038357)
- National Institute of Neurological Disorders and Stroke (R01NS041787, NS041787)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- tau protein, amyloid-beta, axonal transport, GSK3β, Alzheimer's disease, mitochondrial transport, amyloid-beta oligomers, amyloid-beta 42, NMDA receptor, neuronal activity, microtubule binding, Fyn, amyloid precursor protein
- MeSH terms
- Glycogen Synthase Kinase 3 beta, Alzheimer Disease, Animals, Axonal Transport, Enzyme Activation, Humans, Peptide Fragments, Amyloid beta-Peptides, tau Proteins, Mice, Knockout, Glycogen Synthase Kinase 3, Proto-Oncogene Proteins c-fyn, Mice
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