β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

Busciglio, Jorge; Lorenzo, Alfredo; Yeh, John; Yankner, Bruce A

doi:10.1016/0896-6273(95)90232-5

Cited by 595Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

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Busciglio, Jorge, Lorenzo, Alfredo, Yeh, John, Yankner, Bruce A·1995·Neuron

DOI 10.1016/0896-6273(95)90232-5

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Abstract

A central issue in the pathogenesis of Alzheimer's disease (AD) is the relationship between amyloid deposition and neurofibrillary tangle formation. To determine whether amyloid fibril formation affects the phosphorylation state of tau, primary cultures of fetal rat hippocampal and human cortical neurons were treated with beta-amyloid (beta A) in a soluble, amorphous-aggregated, or fibrillar form. Fibrillar beta A, but not soluble or amorphous-aggregated beta A, markedly induces the phosphorylation of tau at Ser-202 and Ser-396/Ser-404, resulting in a shift in the tau M(r) in human cortical neurons. Hyperphosphorylated tau accumulates in the somatodendritic compartment of fibrillar beta A-treated neurons in a soluble form that is not associated with microtubules and is incapable of binding to microtubules in vitro. Dephosphorylation of beta A-induced tau restores its capacity to bind to microtubules. Thus, amyloid fibril formation alters the phosphorylation state of tau, resulting in the loss of microtubule binding capacity and somatodendritic accumulation, properties also exhibited by tau in the AD brain. Amyloid fibril formation may therefore be a cause of abnormal tau phosphorylation in AD.

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From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [35]
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From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [35]

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Background
RETRACTED ARTICLE: Fuzhisan, a Chinese Herbal Medicine, Inhibits Beta-Amyloid-Induced Neurotoxicity and Tau Phosphorylation Through Calpain/Cdk5 Pathway in Cultured Cortical Neurons
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Retracted

Authors: Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A.
Affiliations: Boston Children's Hospital (US)
Brigham and Women's Hospital (US)
ORCID: Busciglio, Jorge
Lorenzo, Alfredo
Yeh, John
Yankner, Bruce A
Venue: Neuron
Publisher: Elsevier BV
Published: 1995-04
Volume: 14
Issue: 4
Pages: 879-888
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/0896-6273(95)90232-5
OpenAlex: W1996917933
Cited by: 595
References: 10
Citations by year: 2026: 8 · 2025: 14 · 2024: 9 · 2023: 11 · 2022: 14 · 2021: 11 · 2020: 14 · 2019: 18 · 2018: 14 · 2017: 12 · 2016: 21 · 2015: 23 · 2014: 23 · 2013: 25 · 2012: 25
FWCI: 13.09
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6682 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (R29AG009229, AG09229)
National Institute of Neurological Disorders and Stroke (R01NS030352, NS30352)
Topics: Health Sciences › Medicine › Physiology › 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: amyloid-beta fibrils, tau phosphorylation, microtubule binding, Alzheimer's disease, neurofibrillary tangles, amyloid deposition, tau dephosphorylation, hippocampal neurons, cortical neurons, tau hyperphosphorylation
MeSH terms: Animals, Cells, Cultured, Cerebral Cortex, Hippocampus, Humans, Microtubules, Neurofibrils, Neurons, Phosphorylation, Phosphoserine, Amyloid beta-Peptides, tau Proteins, Rats

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β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

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