Cited by 364Glycosylation and Glycoproteins ResearchAlzheimer's disease research and treatmentsCarbohydrate Chemistry and Synthesis

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The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine

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Arnold, C. Shane, Johnson, GailV.W., Cole, Robert N., Dong, Dennis L.-Y., Lee, Michael, Hart, Gerald W.·1996·Journal of Biological Chemistry

DOI 10.1074/jbc.271.46.28741

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Abstract

Tau is a family of phosphoproteins that are important in modulating microtubule stability in neurons. In Alzheimer's disease tau is abnormally hyperphosphorylated, no longer binds microtubules, and self-assembles to form paired helical filaments that likely contribute to neuron death. Here we demonstrate that normal bovine tau is multiply modified by Ser(Thr)-O-linked N-acetylglucosamine, a dynamic and abundant post-translational modification that is often reciprocal to Ser(Thr)-phosphorylation. O-GlcNAcylation of tau was demonstrated by blotting with succinylated wheat germ agglutinin and by probing with bovine milk beta(1,4)galactosyltransferase. Structural analyses confirm the linkage and the saccharide structure. Tau splicing variants are multiply O-GlcNAcylated at similar sites, with an average stoichiometry of greater than 4 mol of O-linked N-acetylglucosamine/mol of tau. However, the number of sites occupied appears to be greater than 12, suggesting substoichiometric occupancy at any given site. A similar relationship between average stoichiometry and site-occupancy has also been described for the phosphorylation of tau. Site-specific or stoichiometric changes in O-GlcNAcylation may not only modulate tau function but may also play a role in the formation of paired helical filaments.

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Authors: Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W.
Affiliations: University of Alabama at Birmingham (US)
Corresponding author: Hart, Gerald W.
ORCID: Cole, Robert N.
Lee, Michael
Hart, Gerald W.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1996-11
Volume: 271
Issue: 46
Pages: 28741-28744
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.271.46.28741
OpenAlex: W2066371153
Cited by: 361
References: 61
Citations by year: 2026: 3 · 2025: 12 · 2024: 17 · 2023: 10 · 2022: 12 · 2021: 17 · 2020: 20 · 2019: 13 · 2018: 19 · 2017: 13 · 2016: 18 · 2015: 11 · 2014: 18 · 2013: 12 · 2012: 10
FWCI: 2.15
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by-nc-nd/4.0/ (vor, 8830 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ns027538-10)
National Cancer Institute (R01CA42486, R01CA042486)
National Institute of General Medical Sciences (T32GM008111, 5-T32-GM08111-10)
National Institute of Neurological Disorders and Stroke (R01 NS 27538)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
Keywords: tau protein, O-GlcNAcylation, N-acetylglucosamine, post-translational modification, paired helical filaments, Alzheimer's disease, microtubule binding, phosphorylation, site occupancy
MeSH terms: Acetylglucosamine, Amino Acid Sequence, Animals, Brain Chemistry, Cattle, Galactosyltransferases, Glycosylation, Molecular Sequence Data, Phosphorylation, tau Proteins

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The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine

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