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AKT phosphorylates GSK3 on serine. 27 / 27
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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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"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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"AKT phosphorylates GSK3 on serine 9 for GSK3beta or 21 for GSK3alpha, thereby inactivating GSK3 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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"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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"Thus, reduced Akt activation occurs in conjunction with decreased inhibitory serine-phosphorylation of GSK3 during depressive-like states."

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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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"Both insulin and IGF-1 activate Akt which phosphorylates serine 9 on GSK3β resulting in its inhibition [33, 34]."

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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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"In response to insulin binding, PKB and AKT phosphorylates GSK-3 on serine 9, which prevents the enzyme from phosphorylating glycogen synthase [XREF_BIBR]."

sparser
"Importantly, the phosphorylation of GSK3 at these serine residues by PKB is associated with reduced kinase activity ( xref , xref )."

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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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"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)."

sparser
"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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"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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"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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"However, activated AKT (P-Ser473) usually phosphorylates GSK3β at serine 9, thereby causing inactivation of the protein (reviewed in [3])."

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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."

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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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"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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"Akt phosphorylates GSK3 alpha and beta on inhibitory serine residues 21 and 9, respectively."

sparser
"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 ]."

reach
"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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"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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"Serine 9 of GSK3β can be phosphorylated by AKT and other kinases , leading to GSK-3β 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 - 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)."