Cited by 169Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease

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Guerrero-Muñoz, Marcos J., Gerson, Julia, Castillo-Carranza, Diana L.·2015·Frontiers in Cellular Neuroscience

DOI 10.3389/fncel.2015.00464PMC PMC4667007

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Abstract

Alzheimer's disease (AD) is a progressive disorder in which the most noticeable symptoms are cognitive impairment and memory loss. However, the precise mechanism by which those symptoms develop remains unknown. Of note, neuronal loss occurs at sites where synaptic dysfunction is observed earlier, suggesting that altered synaptic connections precede neuronal loss. The abnormal accumulation of amyloid-β (Aβ) and tau protein is the main histopathological feature of the disease. Several lines of evidence suggest that the small oligomeric forms of Aβ and tau may act synergistically to promote synaptic dysfunction in AD. Remarkably, tau pathology correlates better with the progression of the disease than Aβ. Recently, a growing number of studies have begun to suggest that missorting of tau protein from the axon to the dendrites is required to mediate the detrimental effects of Aβ. In this review we discuss the novel findings regarding the potential mechanisms by which tau oligomers contribute to synaptic dysfunction in AD.

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FIGURE 1 Schematic illustrating the pathological role of tau at dendritic spines. ß-amyloid (Aβ) oligomers directly or indirectly lead to the dystrophic changes in neurites mediated by tau. Hyperphosphorylated tau targets the kinase, Fyn, to the postsynaptic compartment. Fyn phosphorylates NR2B, a subunit of the N-methyl-D-aspartate receptor (NMDAR), resulting in the over-activation of NMDAR, followed by increased concentration of Ca2+ in the cytoplasmic compartment. Aβ oligomers (Aβo) seed tau misfolding and aggregation by direct interaction resulting in tau oligomer formation at dendritic spines. All of these pathways converge in the aggregation of tau protein, spine loss, and consequently, cognitive impairment.CC BY · PubMed Central

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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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“It seems likely that the increase in trimers in treated mice may be a consequence of Aβ∗56 disassembly which has been suggested to be comprised of four Aβ trimers (Lesne et al., 2006).”
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Authors: Guerrero-Muñoz, M. J., Gerson, J., & Castillo-Carranza, D. L.
Affiliations: The University of Texas Medical Branch at Galveston (US)
ORCID: Gerson, Julia
Venue: Frontiers in Cellular Neuroscience
Publisher: Frontiers Media SA
Published: 2015-12-02
Volume: 9
Pages: 464-464
ISSN: 1662-5102 (ISSN-L)
DOI: 10.3389/fncel.2015.00464
PMC: PMC4667007
OpenAlex: W2228598504
Cited by: 168
References: 142
Citations by year: 2026: 9 · 2025: 14 · 2024: 13 · 2023: 13 · 2022: 23 · 2021: 12 · 2020: 23 · 2019: 20 · 2018: 25 · 2017: 9 · 2016: 7
FWCI: 1.68
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Frontiers in Cellular Neuroscience (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: tau oligomers, Alzheimer's disease, synaptic dysfunction, amyloid-beta, tau protein, neurotoxicity, cognitive impairment, memory loss, neuronal loss

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Tau Oligomers: The Toxic Player at Synapses in Alzheimer’s Disease

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