Glycogen synthase kinase 3β is tyrosine phosphorylated by PYK2
Abstract
Glycogen synthase kinase 3beta (GSK3beta) is a Ser/Thr kinase that is involved in numerous cellular activities. GSK3beta is activated by tyrosine phosphorylation. However, very little is known about the tyrosine kinases that are responsible for phosphorylating GSK3beta. In this report, we investigated the ability of the calcium-dependent tyrosine kinase, proline-rich tyrosine kinase 2 (PYK2) to tyrosine phosphorylate GSK3beta. In transfected CHO cells, it was demonstrated that PYK2 tyrosine phosphorylates GSK3beta in situ. The two kinases also coimmunoprecipitated. Furthermore, GSK3beta was tyrosine phosphorylated in vitro by an active, wild type PYK2, but not by the inactive, kinase dead form of PYK2. Therefore, this study is the first to demonstrate that GSK3beta is a substrate of PYK2 both in vitro and in situ.
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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 et al., 2001
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- Authors
- Hartigan, J. A., Xiong, W.-C., & Johnson, G. V. W.
- Affiliations
- University of Alabama at Birmingham (US)
- Corresponding author
- Johnson, Gail V.W.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2001-06
- Volume
- 284
- Issue
- 2
- Pages
- 485-489
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2003720538
- Cited by
- 117
- References
- 29
- Citations by year
- 2026: 7 · 2025: 2 · 2024: 2 · 2023: 7 · 2022: 10 · 2021: 4 · 2020: 3 · 2019: 2 · 2018: 6 · 2017: 4 · 2016: 2 · 2015: 1 · 2014: 4 · 2013: 8 · 2012: 6
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns035060-07)
- National Institute of Neurological Disorders and Stroke (NS35060)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- glycogen synthase kinase-3β, Pyk2, tyrosine phosphorylation, tyrosine kinase, kinase substrates, protein-protein interaction
- MeSH terms
- Animals, Enzyme Activation, Cricetinae, Isoenzymes, Mutation, Phosphorylation, Precipitin Tests, Protein-Tyrosine Kinases, Substrate Specificity, Transfection, Tyrosine, Immunoblotting, CHO Cells, Calcium-Calmodulin-Dependent Protein Kinases, Glycogen Synthase Kinases, Glycogen Synthase Kinase 3, Focal Adhesion Kinase 2
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