Cited by 781Alzheimer's disease research and treatmentsGlycosylation and Glycoproteins ResearchDementia and Cognitive Impairment Research

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O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

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Liu, Fei, Iqbal, Khalid, Grundke-Iqbal, Inge, Hart, Gerald W., Gong, Cheng-Xin·2004·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0400348101PMC PMC490015

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Abstract

Microtubule-associated protein tau is abnormally hyperphosphorylated and aggregated into neurofibrillary tangles in brains of individuals with Alzheimer's disease (AD) and other tauopathies. Tau pathology is critical to pathogenesis and correlates to the severity of dementia. However, the mechanisms leading to abnormal hyperphosphorylation are unknown. Here, we demonstrate that human brain tau was modified by O-GlcNAcylation, a type of protein O-glycosylation by which the monosaccharide β- N -acetylglucosamine (GlcNAc) attaches to serine/threonine residues via an O-linked glycosidic bond. O-GlcNAcylation regulated phosphorylation of tau in a site-specific manner both in vitro and in vivo . At most of the phosphorylation sites, O-GlcNAcylation negatively regulated tau phosphorylation. In an animal model of starved mice, low glucose uptake/metabolism that mimicked those observed in AD brain produced a decrease in O-GlcNAcylation and consequent hyperphosphorylation of tau at the majority of the phosphorylation sites. The O-GlcNAcylation level in AD brain extracts was decreased as compared to that in controls. These results reveal a mechanism of regulation of tau phosphorylation and suggest that abnormal hyperphosphorylation of tau could result from decreased tau O-GlcNAcylation, which probably is induced by deficient brain glucose uptake/metabolism in AD and other tauopathies.

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Authors: Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X.
Affiliations: Johns Hopkins University (US)
Department of Neurochemistry, New York State Institute for Basic Research in Developmental Disabilities, 1050 Forest Hill Road, Staten Island, NY 10314; and Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205
Corresponding author: Gong, Cheng-Xin
ORCID: Liu, Fei
Iqbal, Khalid
Hart, Gerald W.
Gong, Cheng-Xin
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2004-07-12
Volume: 101
Issue: 29
Pages: 10804-10809
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0400348101
PMC: PMC490015
OpenAlex: W2164029759
Cited by: 775
References: 42
Citations by year: 2026: 29 · 2025: 50 · 2024: 38 · 2023: 36 · 2022: 44 · 2021: 63 · 2020: 57 · 2019: 38 · 2018: 46 · 2017: 45 · 2016: 33 · 2015: 23 · 2014: 36 · 2013: 24 · 2012: 35
FWCI: 10.48
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Nanjing Medical University
National Institutes of Health (HD13563)
National Institute on Aging (AG19158, R01AG019158, AG16760, R01AG016760)
Eunice Kennedy Shriver National Institute of Child Health and Human Development (R37HD013563, HD13563)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: O-GlcNAcylation, tau protein, tau hyperphosphorylation, Alzheimer's disease, tauopathy, neurofibrillary tangles, O-glycosylation, glucose metabolism, brain glucose uptake
MeSH terms: Acetylglucosamine, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Brain, Female, Glycosylation, Humans, Male, Mice, Inbred C57BL, Middle Aged, Phosphorylation, Starvation, PC12 Cells, tau Proteins, Rats, Wistar, Mice, Rats, In Vitro Techniques

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O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

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