IndraLab
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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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"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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"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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"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."