IndraLab

Statements

AKT phosphorylates GSK3 on S21. 32 / 41
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"Growth factors, such as EGF, result in inactivation of GSK3 through Ser9 phosphorylation of GSK3α or Ser21 phosphorylation of GSK3β by AKT ."
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"Further, Akt phosphorylates GSK-3 (Ser 21 in GSK-3 α and Ser 9 in GSK-3 β) and suppresses its action, allowing normal cell growth and survival to persist ( Wee and Wang, 2017 )."
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"GSK3 is one of the main targets of Akt and is phosphorylated by active Akt at its two subunits GSK3α (Ser21) and GSK3β (Ser9) ( Manning and Toker, 2017 )."
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"Akt phosphorylates GSK-3 at Serine 21 and Serine 9 in two different isoforms GSK-3 and GSK-3 respectively and inhibits its activity [ xref , xref ]."
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"Recently, we generated homozygous knockin mice in which the PKB phosphorylation site on GSK3α (Ser21) and GSK3β (Ser9) was changed to Ala to prevent inactivation of this enzyme by insulin [5] ."
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"As GSK3 is phosphorylated, and hence inhibited, at Ser9/Ser21 by AKT ( Cohen and Frame, 2001 ), it is tempting to speculate that AKT counteracts CK2-dependent PTEN inactivation through this feedback m[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We next studied the phosphorylation of the inhibitory PKB phosphorylation sites on GSK3α (Ser21) and GSK3β (Ser9) employing phospho-specific antibodies."
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"GSK3 is rapidly phosphorylated at Ser21 in GSK3α or Ser9 in GSK3β by AKT, resulting in inhibition of GSK3 kinase activity [ xref ]."
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"Phosphorylation of GSK3 by AKT at auto-inhibitory N-terminal serine residues (Ser9/Ser21) inhibits GSK3 activity."
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"PKB is known to phosphorylate GSK-3 at Ser 21 in GSK-3α and Ser 9 in GSK-3β."
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"GSK-3 is a substrate of Akt, which phosphorylates GSK-3 on Ser-21, thereby inactivating it ."
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"PKB/Akt phosphorylates GSK3α(Ser-21) and GSK3β(Ser-9), and these residues lie in a typical PKB/Akt consensus substrate motif [14] ."
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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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"AKT phosphorylates GSK3 α or β at Ser21 or Ser9 residue respectively."
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"Akt can phosphorylate GSK3α and GSK3β at residues S21 and S9, respectively, thereby inactivating GSK3 and suppressing β-catenin degradation [144–146]."
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"Furthermore, activated Akt and PKB can induce serine phosphorylation of GSK3 (Ser21 for GSK3alpha; Ser9 for GSK3beta) to inactivate the kinase activity, which subsequently lead to an activation of GS and then increased glycogen synthesis [XREF_BIBR, XREF_BIBR]."
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"We found that Ser 21/9 phosphorylation of GSK-3 was mediated by Ca (2+)/calmodulin-dependent protein kinase II (CaMKII) but not by Akt and PKB, PKA, or p90 (RSK)."
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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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"Akt phosphorylates GSK3β at Ser21 and Ser9 and thereby inactivates this protein kinase."
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"Stimulation of N29/4 cells by insulin for 30 min results in a substantial inhibition of GSK3 activity, as expected from increased PKB activity causing GSK3 Ser-9 and Ser-21 phosphorylation."
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"By contrast, the high-salt diet did not significantly affect Akt expression or its Ser 473 phosphorylation in soleus muscle.GSK-3 is a substrate of Akt, which phosphorylates GSK-3 on Ser 21, thereby i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"GSK-3 serine kinase is directly phosphorylated by Akt on Ser-9 (α-isoform) or Ser-21 (β-isoform), leading to inactivation of GSK-3 kinase ( Laviola et al., 2001 )."
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"Furthermore, activated Akt and PKB can induce serine phosphorylation of GSK3 (Ser21 for GSK3alpha; Ser9 for GSK3beta) to inactivate the kinase activity, which subsequently lead to an activation of GS and then increased glycogen synthesis [XREF_BIBR, XREF_BIBR]."
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"Akt phosphorylates Ser21 of GSK3α and Ser9 of GSK3β resulting in transient inactivation of GSK3β [22, 23]."
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"The activation of AKT causes phosphorylation of GSK3α (Ser 21) and GSK3β (Ser 9) and suppresses their activities."
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"The phosphorylation of GSK-3 by AKT at serine 21 in GSK-3α or serine 9 in GSK-3β inhibits the kinase activity of GSK-3 [ xref , xref ]."
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"This is not surprising as GSK-3α/β isoforms are phosphorylated directly by AKT on S21 and S9 (α and β isoforms respectively), leading to GSK-3 inhibition ."
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"Activated AKT can then phosphorylate the two GSK3 isoforms on their N-terminus (at Ser21 for GSK3α and Ser9 for GSK3β), inactivating them [37, 38]."
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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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"GSK3 is rapidly phosphorylated at Ser21 in GSK3alpha or Ser9 in GSK3beta by AKT, resulting in inhibition of GSK3 kinase activity [XREF_BIBR]."
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"PKB and Akt can phosphorylate both GSK3 isoforms (S21 of GSK3alpha and S9 of GSK3beta), leading to an inhibition of GSK3 activity."
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"PKB and Akt can phosphorylate both GSK3 isoforms (S21 of GSK3alpha and S9 of GSK3beta), leading to an inhibition of GSK3 activity."
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