Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway

Hartigan, Judith A.; Johnson, Gail V.W.

doi:10.1074/jbc.274.30.21395

Cited by 141Alzheimer's disease research and treatmentsProtein Kinase Regulation and GTPase SignalingNeuroscience and Neuropharmacology Research

Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway

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Hartigan, Judith A., Johnson, Gail V.W.·1999·Journal of Biological Chemistry

DOI 10.1074/jbc.274.30.21395

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Abstract

Calcium is a universal intracellular signaling molecule. Through variations in both the amplitude and frequency of intracellular calcium increases, the same calcium ion can elicit different responses. In this report, we investigated the effect of a calcium transient, lasting 2-5 min, on alterations in the phosphorylation state of the cytoskeletal protein, tau. Transient increases in calcium result in a prolonged (1-4 h) approximately 60% increase in tau phosphorylation at the Tau-1 epitope. These increases in tau phosphorylation appear to be more dependent upon the duration of the increase in intracellular calcium and less on the amplitude. The calcium-induced increases in tau phosphorylation are not dependent upon protein synthesis, nor are protein kinase C or calcium/calmodulin-dependent protein kinase II involved in the response. However, the calcium-induced increase in tau phosphorylation was inhibited by lithium, a noncompetitive inhibitor of glycogen synthase kinase-3beta (GSK-3beta), and by the tyrosine kinase inhibitor, genistein. Furthermore, transient increases in calcium resulted in a prolonged increase in GSK-3beta tyrosine phosphorylation concomitant with the increase in tau phosphorylation. Therefore, this study is the first to indicate that transient increases in intracellular calcium result in increased tyrosine phosphorylation and activation of GSK-3beta which subsequently results in a sustained increase in the phosphorylation state of tau.

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Cerebral GSK3β stimulation by phosphorylation at Y216 is mediated by intracellular calcium levels and calcium-dependent PYK2.
“Cerebral GSK3β stimulation by phosphorylation at Y216 is mediated by intracellular calcium levels and calcium-dependent PYK2 (Hartigan and Johnson, 1999; Hartigan et al., 2001; Sayas et al., 2006).”
From APOE3 Christchurch modulates β-catenin/Wnt signaling in iPS cell-derived cerebral organoids from Alzheimer’s cases (2024) · cites this paper as Hartigan and Johnson, 1999

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Authors: Hartigan, J. A., & Johnson, G. V. W.
Affiliations: University of Alabama at Birmingham (US)
Corresponding author: Johnson, Gail V.W.
ORCID: Johnson, Gail V.W.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1999-07
Volume: 274
Issue: 30
Pages: 21395-21401
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.274.30.21395
OpenAlex: W2085663173
Cited by: 141
References: 58
Citations by year: 2025: 5 · 2024: 3 · 2023: 5 · 2022: 3 · 2021: 2 · 2020: 6 · 2019: 6 · 2017: 7 · 2016: 3 · 2015: 5 · 2014: 4 · 2013: 6 · 2012: 8
FWCI: 5.47
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7771 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01ag006569-13)
National Institute on Aging (AG06569)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: calcium transients, tau phosphorylation, glycogen synthase kinase-3β, lithium inhibition, genistein, protein kinase C, calcium/calmodulin-dependent protein kinase II
MeSH terms: Calcium, Humans, Neurons, Phosphorylation, Tumor Cells, Cultured, Signal Transduction, tau Proteins, Calcium-Calmodulin-Dependent Protein Kinases, Glycogen Synthase Kinases, Glycogen Synthase Kinase 3

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Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway

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