Gene interactions and pathways from curated databases and text-mining

◀ Back to INS

GSK3A — INS

Text-mined interactions from Literome

Oriente et al., J Biol Chem 2001 : In these cells, insulin inhibition of GSK3 alpha and -beta requires dual phosphorylation by both Akt/PKB and PKC zeta
Nielsen et al., Am J Physiol Endocrinol Metab 2002 (Glycogen Storage Disease Type V...) : The insulin stimulated increase in Akt phosphorylation was smaller in the McArdle patients than in controls ( 45 +/- 13 vs. 76 +/- 13 %, P < 0.05, respectively ), whereas basal and insulin stimulated glycogen synthase kinase 3alpha and protein phosphatase-1 activities were similar in the two groups
Yamada et al., Am J Physiol Endocrinol Metab 2002 : Overexpression of wt-PDK1 enhanced insulin induced activation of PKB as well as insulin induced phosphorylation of glycogen synthase kinase (GSK)3alpha/beta , a direct downstream target of PKB, although insulin induced glycogen synthesis was not significantly enhanced by wt-PDK1 expression
Miele et al., J Biol Chem 2003 : BDM also blocked the action of HGA on insulin stimulated PKB and GSK3 alpha
Gaster et al., Biochem Biophys Res Commun 2004 (Diabetes Mellitus, Type 2) : However, in myotubes precultured at high insulin concentrations the effect of insulin on GS and GSK-3alpha activity was blunted in both groups
Tang et al., J Biol Chem 2005 (MAP Kinase Signaling System) : Attenuation of PTEN expression by RNAi markedly enhanced insulin stimulated Akt and glycogen synthase kinase 3alpha ( GSK-3alpha ) phosphorylation, as well as deoxyglucose transport in 3T3-L1 adipocytes
Sale et al., Biochemistry 2006 : Knock down of total PKB incompletely blocked insulin stimulated phosphorylation of GSK-3alpha and GSK-3beta, and a pathway involving atypical PKCs, zeta/lambda, was shown to contribute to the signal
Højlund et al., Diabetologia 2006 : Insulin increased Akt phosphorylation at Ser473 and Thr308, inhibited glycogen synthase kinase-3alpha activity, reduced phosphorylation of glycogen synthase at sites 3a+3b, and increased glycogen synthase activity in Arg1174Gln carriers ( all p < 0.05 )
Vahsen et al., Horm Metab Res 2006 (Insulin Resistance) : Insulin regulated serine phosphorylation of Akt and GSK3alpha and GSK3beta was unaltered in heart and skeletal muscle of knockout mice, suggesting unaltered insulin signaling
Shahid et al., J Biol Chem 2007 : Similarly, GRK2 deficiency increased the basal and insulin stimulated phosphorylation of Ser ( 21 ) in glycogen synthase kinase-3alpha
Ciaraldi et al., Endocrinology 2007 (Insulin Resistance) : GSK3alpha overexpression ( 60-100 % increase over control ) did not alter basal GS FV or GU but impaired insulin stimulation of both responses
Fediuc et al., J Cell Physiol 2008 : These effects were accompanied by an increase in basal and insulin stimulated phosphorylation of Akt ( Thr308 ), Akt ( Ser473 ), and GSK3alpha/beta
Chang et al., Fertil Steril 2008 (Insulin Resistance...) : Basal protein levels of glycogen synthase kinase ( GSK3alpha and GSK3beta ) did not differ between control women and women with PCOS, nor did basal or insulin stimulated levels of serine phosphorylated GSK3alpha
Sharma et al., Neurobiol Dis 2008 (Hypercholesterolemia) : The insulin-like growth factor-1 (IGF-1) regulates the glycogen-synthase kinase-3alpha ( GSK-3alpha ) and the insulin degrading enzyme (IDE)
Rao et al., Biochem Biophys Res Commun 1995 (Diabetes Mellitus, Experimental) : The chronic effect of insulin on the expression of the glycogen synthase kinase-3 alpha gene in streptozotocin induced diabetic rat liver is examined