IndraLab

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"In response to insulin, gsk3a inhibited by phosphorylation at ser-21 by pkb/akt1;phosphorylation at this site causes a conformational change, preventing access of substrates to the active site."

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"Similar to SGK1 and protein kinase B (PKB and Akt) isoforms, SGK3 may phosphorylate glycogen synthase kinase GSK3alpha, beta, which has recently been shown to participate in the regulation of basal gastric acid secretion."

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"Protein levels of Akt1 are not affected in the Akt3 KO mice but it is still possible that the observed amplified GSK3alpha and beta phosphorylation is caused by an elevation of Akt1 activity."

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"The data presented here suggests that constitutive AKT1 and 3 but not AKT2 activity are sufficient to phosphorylate GSK3alpha, while all three isoforms are sufficient in phosphorylating GSK3beta."

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"GSK-3 activity is inhibited through phosphorylation of serine 21 in GSK-3 alpha and serine 9 in GSK-3 beta. These serine residues of GSK-3 have been previously identified as targets of protein kinase B (PKB/Akt), a serine/threonine kinase located downstream of phosphatidylinositol 3-kinase. "

"glycogen synthase kinase GSK3 which itself is a target of protein kinase B (PKB) and the serum and glucocorticoid inducible kinase SGK1. Phosphorylation of GSK3 by PKB or SGK1 inhibits GSK3 activity an the present study explored whether mineralocorticoid excess had any effect on the phosphorylation status of the a and beta isoforms of GSK3. Western blotting using an antibody specific for the PKB/SGK1 consensus phosphorylation site in GSK3a/beta (serine 21 and 9 respectively) revealed an increase in GSK3a/beta phosphorylation in human embryonic kidney 293 (HEK293) cells overexpressing wild type SGK1, constitutively active SGK1, but not catalytically inactive SGK1. The effect of SGK1 was mimicked by PKB and SGK3."

"Modified assertion"

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"Inhibition of PKC zeta activity, however, reduced Akt/PKB phosphorylation of the key serine sites on GSK3 alpha and -beta by >80% (p < 0.001) and prevented full GSK3 inactivation by insulin."