IndraLab
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"Li is a monovalent cation that is capable of inhibiting GSK3 both directly, via competition with its cofactor magnesium, and indirectly, via activation of the PI3K/Akt pathway, which phosphorylates GSK3 at the Ser 21 (GSK3α) and Ser 9 (GSK3β) sites, preventing substrate binding to the GSK3 isoforms (Hamstra, Whitley, et al., 2020)."
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"We found FGF1 binds to the FGFR, resulting in the phosphorylation of Akt, which in turn phosphorylates GSK3β at Ser9, rendering the kinase-inactive and resulting in decreased phosphorylation of downstream substrates, including β-catenin.Although Tian-Song Liang has found that MicroRNA-506 can inhibit NPC tumour growth and metastasis by downregulating LHX2 [44], our study further extended the downstream targets and signalling pathway by which LHX2 serve as the oncogene in NPC, providing potential therapeutic strategies, such as FGF1/FGFR inhibitors."
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"Axin, APC, GSK3β, and CK1α formed a destruction complex in the cytoplasm.11, 12 When the destruction complex interacted with β‐catenin, β‐catenin was ubiquitinated and subsequently degraded by cellular proteasome.13, 14 In addition, as a phosphorylation substrate of Akt, GSK3β could be phosphorylated by Akt at Ser9, which inactivated GSK3β, leading to inhibition of β‐catenin degradation by proteasome."
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"Interestingly, corylin did not directly inhibit the binding of HSP90β to SREBPs but disrupted the interaction between HSP90β and Akt and significantly reduced Thr308 phosphorylation of Akt and Ser9 phosphorylation of GSK3β, thereby promoting F‐Box‐ and WD40 domain protein‐7‐mediated ubiquitination and proteasomal degradation of mature SREBPs.In preclinical models, corylin treatment effectively improved Western‐type diet‐induced dyslipidemia, insulin resistance, and atherosclerosis in mice by inhibiting HSP90β."
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"More recently, GSK3 was shown to enhance proteasomal degradation of VEGFR-2 by regulating the binding of β-transducin repeats containing E3 ubiquitin protein ligase to VEGFR-2 (29), and GSK3 activity is inhibited by AKT that phosphorylates the serine residues Ser21 in GSK3α and Ser9 in GSK3β (30)."
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"The activated Akt and p70S6K further phosphorylate GSK3β at ser9 and reduces its activity, which promotes the activation of glycogen synthase (GS), thus increasing the muscle glycogen.In addition to muscle mechanisms for insulin resistance, central body fat (visceral fat and subcutaneous abdominal fat) is associated with insulin resistance [20,39]."
| PMC
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"For instance, two pancreatic cancer cell lines, PANC1 and ASPC1, exhibit amplification of AKT and high levels of AKT RNA and protein [XREF_BIBR] but also highly active GSK-3beta suggesting that, although some pools of GSK-3 can be phosphorylated by AKT at Ser21 and Ser9 and inhibited, other pools of GSK-3 may remain active in cancer cells [XREF_BIBR]."
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"The apoptosis-related factors (cleaved PARP and caspase-3) and cell cycle arrest-related factors (p21 and p27) showed the same trend, whereas the suppression of Akt phosphorylation and induction of GSK3β inactivation due to increased Ser9 phosphorylation after the TA3 treatment was blocked by insulin."
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"We found that AKT phosphorylation resulted in an increased phosphorylation of GSK3β in its Ser9 and consequently, leads to an up-regulation of SNAI1, which undergoes degradation when phosphorylated by active GSK3β [43] both in terms of protein level (Fig. 4b) and of mRNA (as shown below, Fig. 4d)."
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"While AKT activity can be suppressed by DISC1 due to its competitive binding to Girdin, the AKT co-activator [36], we found that the AKT pathway is activated by DISC-Δ3 variant lacking the Girdin binding region, thus resulting in an indirect enhancement of GSK3β S9 phosphorylation."
rlimsp
"The critical protein in the regulation of β-catenin phosphorylation and stability is GSK-3, whose activity is also regulated by phosphorylation at serine 9. Although PKB can phosphorylate GSK-3 at this site and inhibit its activity, our results also implicate a direct role for ILK in the regulation of GSK-3 activity."
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"50 In turn, Akt-dependent phosphorylation of GSK3β at S9 inactivates the kinase.51 Thus, REDD1 enhances NLRP3 inflammasome activation via an Akt/GSK3β/NF-κB signaling axis.In the retina of diabetic mice treated with the GSK3 inhibitor VP3.15, NLRP3 expression was not increased as compared with nondiabetic control mice."
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"In contrast, in growth factor/insulin signaling, the kinases PKA and PKB/Akt phosphorylate GSK3β at Ser9 (Cross et al., 1995; Fang et al., 2000; Jensen et al., 2007; Sutherland et al., 1993), which inhibits GSK3β by binding in the priming pocket and blocking substrate binding (Dajani et al., 2001; Frame and Cohen, 2001; Stamos et al., 2014; ter Haar et al., 2001; Figure 1A)."