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AKT phosphorylates GSK3 on serine. 77 / 82
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"GSK3β is phosphorylated by AKT in serine 9 leading to the inactivation of GSK3β."
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"Phosphorylation of serine residues in GSK3 (ser-9 for GSK3β and ser-21 for GSK3α) by Akt inhibits GSK3 kinase activity, and inhibition of GSK3 has been shown to decrease blood glucose levels and to increase glucose clearance rates ( xref ; xref )."
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"GSK-3 itself is phosphorylated by serine kinase Akt and thus regulated by the PI3K-Akt pathway [ 28 ]."
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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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"Insulin signaling activates PI3K and Akt that lead to enhancing the inhibitory serine phosphorylation of GSK3."
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"We considered the involvement of GSK3β, which is phosphorylated at serine-9 by growth factor-stimulated Akt kinase, resulting in its autoinhibition [26,27] ."
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"Interestingly, Par3 can directly bind to PI3K and enhance its activity, suggesting that increased serine phosphorylation of GSK3 by Akt might be downstream of GSK3 inactivation by Par3."
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"Expression of dominant negative Akt kinase significantly inhibited PDGF-induced phosphorylation of GSK3β at serine-9 ( Fig. 4 A, bottom, compare lane 4 with lane 2)."
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"Akt phosphorylation of GSK3β (on serine-9) leads to its inactivation."
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"Serine 9 of GSK3β can be phosphorylated by AKT and other kinases , leading to GSK-3β inactivation."
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"The Akt signaling pathway often is a major regulator of GSK-3 because Akt phosphorylates GSK-3 on these inhibitory serine residues, which has been shown to involved in dopamine signaling and many aspects of psychiatric disorders [XREF_BIBR]."
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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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"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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"Multiple signaling pathways feed into this site to increase the serine-phosphorylation of GSK-3, which can be mediated by AKT, protein kinase A (PKA), protein kinase C, p70 S6 kinase, and other kinase[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Akt, which is downstream of PI3K, seems to be involved in this action since the pharmacological inhibition of Akt produces a decrease in the serine 9 inhibitory phosphorylation of GSK3β and a dose-dep[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Phosphorylation of GSK3 by Akt at N-terminal serine residue inhibits its activity towards protein translation and cell growth [167] ."
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"PKB subsequently phosphorylates glycogen synthase kinase -3 (GSK-3) at an N-terminal serine residue (Ser 21 on GSK-3alpha and Ser 9 on GSK-3beta) rendering it inactive [XREF_BIBR, XREF_BIBR]."
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"In contrast to the activating phosphorylation of Akt, the phosphorylation of GSK3 that we measured (at Ser of GSK3α and Ser of GSK3β, catalyzed by Akt) inhibits the kinase activity of GSK3 (24)."
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"Phosphorylation of GSK3 by AKT at auto-inhibitory N-terminal serine residues (Ser9/Ser21) inhibits GSK3 activity."
30503054
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"In the following decades, it was found that engagement of insulin receptor by insulin activates the phosphatidylinositol 3-kinase (PI3K)–Akt pathway, leading to phosphorylation of GSK3 by Akt at a serine residue near the N terminus of GSK3."
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"GSK3β is a downstream kinase of AKT, and GSK3β phosphorylation at serine-9 (S9) by AKT and other members of the AGC kinase family results in the loss of function of GSK3β ( van Weeren et al., 1998 )."
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"In suspension, phosphorylated β-catenin was reduced to undetectable levels, likely due to its rapid degradation induced by loss of cell attachment.The activity of protein kinase B (Akt), a key serine/[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"AKT is a serine-threonine protein kinase which exists in three isoforms: AKT1 and AKT2, ubiquitously expressed, and AKT3 which is predominantly expressed in the brain, kidney and heart.Activated AKT p[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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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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"Importantly, the phosphorylation of GSK3 at these serine residues by PKB is associated with reduced kinase activity ( xref , xref )."
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"In our previous study, we demonstrated that the phosphorylation of GSK3β at serine 9 by activated AKT plays a role in the hair-inductive properties of DP cells via the activation of Wnt/β-catenin signaling, which is one of the most important signaling pathways for hair growth in HFs [12]."
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"Lithium ions activate phosphatidylinositol 3 (PI3) kinase and its downstream effector Protein kinase B (AKT), which in turn phosphorylates a critical serine residue in GSK3, leading to its inactivatio[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Since Akt phosphorylates GSK3β on its regulatory serine residue (Serine9), inhibiting its activity [34], increased p-GSK3β (Serine9) in FI animals compared to F rats could be a consequence of the recovery in p-Akt level induced by the phytochemical."
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"This is where activated Akt activates the serine phosphorylation of GSK3β to an inactive form, removing the inhibition of GS, which ultimately increases glycogen synthesis and improves insulin resista[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"AKT phosphorylates GSK3β at serine 9, inhibiting its function and stabilizing β-catenin [36,37]."
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"AKT phosphorylates GSK3 on serine 9 for GSK3beta or 21 for GSK3alpha, thereby inactivating GSK3 XREF_BIBR."
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"Thus, reduced Akt activation occurs in conjunction with decreased inhibitory serine-phosphorylation of GSK3 during depressive-like states."
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"Phosphorylation at Serine 9 of GSK3β is mainly mediated by AKT (Wakatsuki et al., 2011), while PI3K-AKT signaling was enriched in our KEGG analysis."
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"RANKL-activated AKT enhanced GSK3β phosphorylation at serine 9, causing its inactivation, increasing NFATc1 accumulation in the nucleus, and promoting osteoclastogenesis (37)."
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"AKT can phosphorylate GSK3β at serine 9 and inactivate it, in response to active IS."
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"Furthermore Akt regulates the storage of glucose in the form of glycogen by phosphorylating GSK-3 on a serine residue at the N-terminus (GSK-3α Ser21 and GSK-3β Ser9), resulting in inhibition of its k[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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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_BIBR, XREF_BIBR]."
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"Activation of Akt may contribute a part of the drug-induced increases in serine-phosphorylation of GSK3, but it appears not to be sufficiently robust to account entirely for the increased phosphorylat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Protein kinase B also called Akt, phosphorylates GSK3β at serine 9, and GSK3β thereby becomes inactive, which leads to cardiac hypertrophy [3] ."
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"Insulin signaling facilitates PI3 kinase activation, which will eventually lead to the phosphorylation of GSK3β and GSK3α serine at positions 9 and 21 by AKT."
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"AKT regulates the storage of glucose in the form of glycogen by phosphorylating GSK-3 at N-terminal serine residues (GSK-3α Ser21 and GSK-3β Ser9), thereby inhibiting its kinase activity."
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"Interestingly, Akt can interact with GSK3β and phosphorylate GSK3β on serine 9 to inactivate GSK3β (van Weeren et al., 1998), implying that perhaps Akt, GSK3β, and PS can form a complex."
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"Moreover, Akt phosphorylates and inactivates the glycogen synthase kinase Gsk3β at Serine 9."
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"Akt phosphorylates GSK3 alpha and beta on inhibitory serine residues 21 and 9, respectively."
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"In response to insulin binding, PKB and AKT phosphorylates GSK-3 on serine 9, which prevents the enzyme from phosphorylating glycogen synthase [XREF_BIBR - XREF_BIBR]."
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"In response to insulin binding, PKB and AKT phosphorylates GSK-3 on serine 9, which prevents the enzyme from phosphorylating glycogen synthase [XREF_BIBR - XREF_BIBR]."
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"Akt can phosphorylate GSK3 on serine residues, leading to the inhibition of its activity [33] ."
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"The activated Akt phosphorylates GSK3β on serine 9, which constitutively inactivates GSK3β and thus leads to a decrease in microtubule stability [39] ."
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"Multiple signaling pathways feed into this site to increase the serine phosphorylation of GSK3, which can be mediated by Akt, protein kinase A (PKA), protein kinase C, p70 S6 kinase, and other kinases."
25435019
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"In the following decades, it was found that engagement of insulin receptor by insulin activates the phosphatidylinositol 3-kinase (PI3K)–Akt pathway, leading to phosphorylation of GSK3 by Akt at a serine residue near the N terminus of GSK3."
34623920
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"Lithium ions activate phosphatidylinositol 3 (PI3) kinase and its downstream effector Protein kinase B (AKT), which in turn phosphorylates a critical serine residue in GSK3, leading to its inactivatio[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Both, SGK and AKT, were able to phosphorylate the N-terminus of GSK-3, serine-21 on GSK3-α, and serine-9 on the β-isoform ( Failor et al., 2007 ), but were not affected by 1,8-cineol."
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"GSK-3 is activated during brain stroke, whereas GSK-3 inactivation, through serine phosphorylation of GSK-3 by PI3K/Akt activation to block glutamate-induced Akt inactivation, protects the brain by promoting angiogenesis, neurogenesis, anti-apoptosis, and anti-inflammation [11]."
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"Direct phosphorylation of GSK-3 by PKB on a serine residue (Ser9 in GSK-3beta and Ser21 in GSK-3alpha) inhibits the activity of the enzyme [19]."
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"GSK3β is part of several signal transduction pathways and is involved in the signaling induced by kinases such as AKT, which phosphorylates GSK3β at serine 9, or AMPK, i.e., kinases, for which a mitochondrial localization has been described (see text and [50]) and that contribute to myocardial I/R injury and the protection from it."
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"Serine phosphorylation of GSK3 (pSGSK3), catalyzed by Akt, renders GSK3 inactivation [XREF_BIBR], whereas tyrosine phosphorylation of GSK3 (pYGSK3) results in an active form of the enzyme."
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"GSK3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser of GSK3α and Ser of GSK3β."
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"These mediators activate phosphatidylinositol-3-kinase (PI3K) and Akt which phosphorylates GSK3 at an amino terminal serine residue (Ser21 on GSK3alpha and Ser9 on GSK3beta) creating a pseudo-substrate motif that inhibits the enzyme 's activity and allows activation of downstream effectors like glycogen synthase and the mammalian target of rapamycin (mTOR)."
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"Activated PKB increases serine phosphorylation of GSK3 leading to its inhibition and activation of GS."
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"The inhibition of GSK3β activity is principally effectuated by Akt, the most proximal and hegemonial kinase that phosphorylates GSK3β at the Ser residue [49]."
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"In response to insulin stimulation, Akt can lead to a decrease in GSK3α/β activity by phosphorylating serine 21 of GSK3α and serine 9 of GSK3β (Patel and Werstuck, 2021)."
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"The two isoforms of GSK-3, GSK-3alpha and GSK-3beta, can be phosphorylated on serine 21 and serine 9, respectively, by Akt kinases."
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"Once activated, Akt in turn phosphorylates GSK3 isoforms at the single regulatory serine residues serine 21 (GSK3alpha) and serine 9 (GSK3beta) that are located in the N-terminal domains of both GSK3alpha and GSK3beta and thereby causing their inactivation."
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"In response to insulin binding, PKB and AKT phosphorylates GSK-3 on serine 9, which prevents the enzyme from phosphorylating glycogen synthase [XREF_BIBR]."
25885803
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"In response to insulin binding, PKB and AKT phosphorylates GSK-3 on serine 9, which prevents the enzyme from phosphorylating glycogen synthase [XREF_BIBR]."
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"In its active state, when phosphorylated at Ser (pAkt ), Akt phosphorylates GSK3β at Ser (Hermida et al., 2017) leading to GSK3β inactivation."
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"Both insulin and IGF-1 activate Akt which phosphorylates serine 9 on GSK3β resulting in its inhibition [33, 34]."
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"Insulin, neurotrophins, and other growth factors activate phosphatidylinositol-3-kinase (PI3K) and Akt which phosphorylates GSK-3 at an N-terminal serine residue."
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"Phosphorylation of GSK3 by Akt at N-terminal serine residue inhibits its activity towards protein translation and cell growth [167] ."
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"However, activated AKT (P-Ser473) usually phosphorylates GSK3β at serine 9, thereby causing inactivation of the protein (reviewed in [3])."
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"Akt phosphorylates GSK3 alpha and beta on inhibitory serine residues 21 and 9 respectively."
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"Akt phosphorylates GSK3β on serine 9, promoting GSK3β inactivation ( Khaled et al., 2002 )."
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"PI3K/AKT pathway phosphorylates GSK3β in the serine phosphorylation site (inactive the GSK3β), which is closely associated with the phosphorylation of the microtubule-associated protein Tau, a hallmar[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Glycogen synthase kinase 3 (GSK3) phosphorylates the N-terminal phosphodegron in TAZ, increasing its binding to the Skp1-Cullin-F-box (SCF) subunit of E3 Ub ligase, βTrCP, leading to TAZ ubiquitylation and degradation.38 GSK3 activity is suppressed by AKT phosphorylating serine 9 in GSK3β.39 We found leader cells exhibited higher GSK3β phosphorylation than follower cells that correlated with their elevated pAKT expression (Figure 5C)."
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"In the present study, GSK3β was identified as a tumor suppressor in PC-9G cells without EGFR mutations, suggesting that the role of GSK3β may vary according to whether EGFR is mutated or not in gefitinib-resistant NSCLC.The PI3K/AKT pathway serves a key role in cancer cells that are resistant to EGFR-TKIs (22,32), and AKT phosphorylates GSK3β at serine 9 (33,34)."
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"The Akt signaling pathway often is a major regulator of GSK-3 because Akt phosphorylates GSK-3 on these inhibitory serine residues, which has been shown to involved in dopamine signaling and many aspects of psychiatric disorders [ xref ]."
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"Akt can phosphorylate GSK3 on serine residues, leading to the inhibition of its activity [33] ."
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