GSK3 as a Master Regulator of Cellular Processes
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References
- Embi, N.; Rylatt, D.B.; Cohen, P. Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent protein kinase and phosphorylase kinase. Eur. J. Biochem. 1980, 107, 519–527. [Google Scholar] [CrossRef]
- Woodgett, J.R. Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J. 1990, 9, 2431–2438. [Google Scholar] [CrossRef]
- Sutherland, C. What Are the bona fide GSK3 Substrates? Int. J. Alzheimer’s Dis. 2011, 2011, 505607. [Google Scholar]
- McCubrey, J.A.; Fitzgerald, T.L.; Yang, L.V.; Lertpiriyapong, K.; Steelman, L.S.; Abrams, S.L.; Montalto, G.; Cervello, M.; Neri, L.M.; Cocco, L.; et al. Roles of GSK-3 and microRNAs on epithelial mesenchymal transition and cancer stem cells. Oncotarget 2017, 8, 14221–14250. [Google Scholar] [CrossRef]
- Patel, P.; Woodgett, J.R. Glycogen Synthase Kinase 3: A Kinase for All Pathways? Curr. Top. Dev. Biol. 2017, 123, 277–302. [Google Scholar]
- Hoffmeister, L.; Diekmann, M.; Brand, K.; Huber, R. GSK3: A Kinase Balancing Promotion and Resolution of Inflammation. Cells 2020, 9, 820. [Google Scholar] [CrossRef]
- Albrecht, L.V.; Tejeda-Munoz, N.; De Robertis, E.M. Cell Biology of Canonical Wnt Signaling. Annu. Rev. Cell Dev. Biol. 2021, 37, 369–389. [Google Scholar] [CrossRef]
- Li, C.; Furth, E.E.; Rustgi, A.K.; Klein, P.S. When You Come to a Fork in the Road, Take It: Wnt Signaling Activates Multiple Pathways through the APC/Axin/GSK-3 Complex. Cells 2023, 12, 2256. [Google Scholar] [CrossRef]
- Beurel, E.; Grieco, S.F.; Jope, R.S. Glycogen synthase kinase-3 (GSK3): Regulation, actions, and diseases. Pharmacol. Ther. 2015, 148, 114–131. [Google Scholar] [CrossRef]
- Wagner, F.F.; Benajiba, L.; Campbell, A.J.; Weiwer, M.; Sacher, J.R.; Gale, J.P.; Ross, L.; Puissant, A.; Alexe, G.; Conway, A.; et al. Exploiting an Asp-Glu “switch” in glycogen synthase kinase 3 to design paralog-selective inhibitors for use in acute myeloid leukemia. Sci. Transl. Med. 2018, 10, eaam8460. [Google Scholar] [CrossRef]
- Thornton, T.M.; Pedraza-Alva, G.; Deng, B.; Wood, C.D.; Aronshtam, A.; Clements, J.L.; Sabio, G.; Davis, R.J.; Matthews, D.E.; Doble, B.; et al. Phosphorylation by p38 MAPK as an alternative pathway for GSK3β inactivation. Science 2008, 320, 667–670. [Google Scholar] [CrossRef] [PubMed]
- Jope, R.S.; Cheng, Y.; Lowell, J.A.; Worthen, R.J.; Sitbon, Y.H.; Beurel, E. Stressed and Inflamed, Can GSK3 Be Blamed? Trends Biochem. Sci. 2017, 42, 180–192. [Google Scholar] [CrossRef] [PubMed]
- Calvo, B.; Fernandez, M.; Rincon, M.; Tranque, P. GSK3β Inhibition by Phosphorylation at Ser389 Controls Neuroinflammation. Int. J. Mol. Sci. 2022, 24, 337. [Google Scholar] [CrossRef] [PubMed]
- Calvo, B.; Thornton, T.M.; Rincon, M.; Tranque, P.; Fernandez, M. Regulation of GSK3β by Ser389 Phosphorylation During Neural Development. Mol. Neurobiol. 2021, 58, 809–820. [Google Scholar] [CrossRef] [PubMed]
- Skrzypczak-Wiercioch, A.; Salat, K. Lipopolysaccharide-Induced Model of Neuroinflammation: Mechanisms of Action, Research Application and Future Directions for Its Use. Molecules 2022, 27, 5481. [Google Scholar] [CrossRef]
- Jiang, H.; Li, L.; Zhang, L.; Zang, G.; Sun, Z.; Wang, Z. Role of endothelial cells in vascular calcification. Front. Cardiovasc. Med. 2022, 9, 895005. [Google Scholar] [CrossRef]
- Cai, X.; Zhao, Y.; Yang, Y.; Wu, X.; Zhang, L.; Ma, J.A.; Ji, J.; Bostrom, K.I.; Yao, Y. GSK3β Inhibition Ameliorates Atherosclerotic Calcification. Int. J. Mol. Sci. 2023, 24, 11638. [Google Scholar] [CrossRef]
- Bostrom, K.I.; Qiao, X.; Zhao, Y.; Wu, X.; Zhang, L.; Ma, J.A.; Ji, J.; Cai, X.; Yao, Y. GSK3β Inhibition Reduced Vascular Calcification in Ins2Akita/+ Mice. Int. J. Mol. Sci. 2023, 24, 5971. [Google Scholar] [CrossRef]
- Mastrogiacomo, L.; Werstuck, G.H. Investigating the Role of Endothelial Glycogen Synthase Kinase3α/β in Atherogenesis in Low Density Lipoprotein Receptor Knockout Mice. Int. J. Mol. Sci. 2022, 23, 14780. [Google Scholar] [CrossRef]
- Sag, C.M.; Schnelle, M.; Zhang, J.; Murdoch, C.E.; Kossmann, S.; Protti, A.; Santos, C.X.C.; Sawyer, G.; Zhang, X.; Mongue-Din, H.; et al. Distinct Regulatory Effects of Myeloid Cell and Endothelial Cell NAPDH Oxidase 2 on Blood Pressure. Circulation 2017, 135, 2163–2177. [Google Scholar] [CrossRef]
- Banko, N.S.; McAlpine, C.S.; Venegas-Pino, D.E.; Raja, P.; Shi, Y.; Khan, M.I.; Werstuck, G.H. Glycogen synthase kinase 3α deficiency attenuates atherosclerosis and hepatic steatosis in high fat diet-fed low density lipoprotein receptor-deficient mice. Am. J. Pathol. 2014, 184, 3394–3404. [Google Scholar] [CrossRef] [PubMed]
- McAlpine, C.S.; Huang, A.; Emdin, A.; Banko, N.S.; Beriault, D.R.; Shi, Y.; Werstuck, G.H. Deletion of Myeloid GSK3α Attenuates Atherosclerosis and Promotes an M2 Macrophage Phenotype. Arterioscler. Thromb. Vasc. Biol. 2015, 35, 1113–1122. [Google Scholar] [CrossRef] [PubMed]
- Shenker, B.J.; Walker, L.P.; Zekavat, A.; Korostoff, J.; Boesze-Battaglia, K. Aggregatibacter actinomycetemcomitans Cytolethal Distending Toxin-Induces Cell Cycle Arrest in a Glycogen Synthase Kinase (GSK)-3-Dependent Manner in Oral Keratinocytes. Int. J. Mol. Sci. 2022, 23, 11831. [Google Scholar] [CrossRef] [PubMed]
- Loxha, L.; Ibrahim, N.K.; Stasche, A.S.; Cinar, B.; Dolgner, T.; Niessen, J.; Schreek, S.; Fehlhaber, B.; Forster, M.; Stanulla, M.; et al. GSK3α Regulates Temporally Dynamic Changes in Ribosomal Proteins upon Amino Acid Starvation in Cancer Cells. Int. J. Mol. Sci. 2023, 24, 13260. [Google Scholar] [CrossRef] [PubMed]
- Zhang, J.B.; Lu, Z.J.; Yu, H.Z. Silencing of Glycogen Synthase Kinase 3 Significantly Inhibits Chitin and Fatty Acid Metabolism in Asian Citrus Psyllid, Diaphorina citri. Int. J. Mol. Sci. 2022, 23, 9654. [Google Scholar] [CrossRef] [PubMed]
- Pons, B.J.; Vignard, J.; Mirey, G. Cytolethal Distending Toxin Subunit B: A Review of Structure-Function Relationship. Toxins 2019, 11, 595. [Google Scholar] [CrossRef] [PubMed]
- Shenker, B.J.; Boesze-Battaglia, K.; Scuron, M.D.; Walker, L.P.; Zekavat, A.; Dlakic, M. The toxicity of the Aggregatibacter actinomycetemcomitans cytolethal distending toxin correlates with its phosphatidylinositol-3,4,5-triphosphate phosphatase activity. Cell. Microbiol. 2016, 18, 223–243. [Google Scholar] [CrossRef]
- Hinze, L.; Pfirrmann, M.; Karim, S.; Degar, J.; McGuckin, C.; Vinjamur, D.; Sacher, J.; Stevenson, K.E.; Neuberg, D.S.; Orellana, E.; et al. Synthetic Lethality of Wnt Pathway Activation and Asparaginase in Drug-Resistant Acute Leukemias. Cancer Cell 2019, 35, 664–676. [Google Scholar] [CrossRef]
- Arnould, T.; Michel, S.; Renard, P. Mitochondria Retrograde Signaling and the UPR mt: Where Are We in Mammals? Int. J. Mol. Sci. 2015, 16, 18224–18251. [Google Scholar] [CrossRef]
- Mishra, S.; Ghanim, M. Interactions of Liberibacter Species with Their Psyllid Vectors: Molecular, Biological and Behavioural Mechanisms. Int. J. Mol. Sci. 2022, 23, 4029. [Google Scholar] [CrossRef]
- Kim, J.H.; Creekmore, E.; Vezina, P. Microinjection of CART peptide 55–102 into the nucleus accumbens blocks amphetamine-induced locomotion. Neuropeptides 2003, 37, 369–373. [Google Scholar] [CrossRef] [PubMed]
- Cho, B.R.; Kim, W.Y.; Jang, J.K.; Lee, J.W.; Kim, J.H. Glycogen Synthase Kinase 3β Is a Key Regulator in the Inhibitory Effects of Accumbal Cocaine- and Amphetamine-Regulated Transcript Peptide 55–102 on Amphetamine-Induced Locomotor Activity. Int. J. Mol. Sci. 2022, 23, 15633. [Google Scholar] [CrossRef] [PubMed]
- Kim, W.Y.; Jang, J.K.; Lee, J.W.; Jang, H.; Kim, J.H. Decrease of GSK3β phosphorylation in the rat nucleus accumbens core enhances cocaine-induced hyper-locomotor activity. J. Neurochem. 2013, 125, 642–648. [Google Scholar] [CrossRef] [PubMed]
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Lichtinghagen, R.; Huber, R. GSK3 as a Master Regulator of Cellular Processes. Int. J. Mol. Sci. 2023, 24, 15503. https://doi.org/10.3390/ijms242115503
Lichtinghagen R, Huber R. GSK3 as a Master Regulator of Cellular Processes. International Journal of Molecular Sciences. 2023; 24(21):15503. https://doi.org/10.3390/ijms242115503
Chicago/Turabian StyleLichtinghagen, Ralf, and René Huber. 2023. "GSK3 as a Master Regulator of Cellular Processes" International Journal of Molecular Sciences 24, no. 21: 15503. https://doi.org/10.3390/ijms242115503