Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis

By Edward J. Mcmanus, K. Sakamoto, L. Armit, Leah Ronaldson, N. Shpiro, R. Marquez, D. Alessi. EMBO Journal, 2005

647 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/032849400541c8fbf13da3f689888a07e65638e2

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Citations in the corpus

• Glycogen synthase kinase-3 (GSK3): regulation, actions, and diseases (2014, methodology): “The importance of inhibition of GSK3 by serine-phosphorylation in mood disorders has been further verified in animal models by using GSK3 knockin mice developed by the Alessi laboratory (McManus et al., 2005), with the regulatory serines of GSK3 mutated to alanines.”
• Functional redundancy of GSK-3α and GSK-3β in wnt/β-catenin signaling shown by using an allelic series of embryonic stem cell lines (2007, background): “Most conclusively, mice in which both GSK-3α and β were genetically manipulated so that they expressed only S9A/S21A mutant alleles of GSK-3β and α, respectively, are viable, fertile and grossly normal (McManus et al., 2005).”
• The nuts and bolts of AGC protein kinases (2010, background): “Akt also stimulates glycogen synthesis by phosphorylating and inhibiting glycogen synthase kinase 3, resulting in the dephosphorylation and activation of glycogen synthas”
• Glycogen and its metabolism: some new developments and old themes. (2012, background): “[174], discussed above, on the double-knockin homozygous mice with constitutively active GSK3 in which glycogen levels were normal.”
• GSK3 signaling in neural development (2010, background): “However, mutant mice (GSK3α-Ser21Ala/GSK3β-Ser9Ala double knock-in mice) with GSK3s that cannot be phosphorylated at their N-termini developed normally with no overt phenotype in the nervous system (although insulin-induced activation of glycogen synthase was disrupted in the muscle”
• The β-catenin destruction complex. (2013, background): “Although autoinhibition by the phosphorylated amino-terminal peptide is important in non-Wnt GSK-3 functions, mutation of the Ser21/Ser9 does not affect Wnt signaling, and this residue does not become phosphorylated on Wnt stimulation (Ding et al. 2000; McManus et al. 2005).”
• Osteocytes, mechanosensing and Wnt signaling. (2008, background): “The alpha isoform (GSK-3α) can also be phosphorylated (at serine-21) and may also play a role in controlling β–catenin levels (80)(7).”
• Regulation of insulin sensitivity by serine/threonine phosphorylation of insulin receptor substrate proteins IRS1 and IRS2 (2012, background): “Comparison of knock-in mice with constitutively active GSK3 isoforms (α, β, or α and β) demonstrates the predominance of GSK3β in muscle, yet none of these mice show impaired AKT activation or become diabetic [140].”