◀ Back to PI3

PI3 — SLC2A4

Text-mined interactions from Literome

Zhou et al., Mol Endocrinol 1999 : Because phosphatidylinositol (PI) 3-kinase is essential for insulin stimulated translocation of GLUT4 , we also studied a mutant IRS-3 molecule ( IRS-3-F4 ) in which Phe was substituted for Tyr in all four YXXM motifs ( the phosphorylation sites predicted to bind to and activate PI 3-kinase )
Kim et al., Diabetes 1999 (Hyperinsulinism) : Activation of phosphoinositide (PI) 3-kinase is necessary for insulin stimulated GLUT4 translocation, and the serine/threonine kinase Akt/protein kinase B (PKB) is a downstream mediator of some actions of PI 3-kinase
Wang et al., Biochem J 2000 : Activation of phosphoinositide 3-kinase (PI-3K) is essential for insulin stimulated translocation of GLUT4 and glucose transport in insulin target tissues ... We asked whether the stimulation of G ( i ) -coupled receptors would trigger GLUT4 translocation and glucose uptake by the activation of Gbetagamma dependent p110gamma PI-3K
Ishibashi et al., Endocrinology 2000 : We have recently shown that pretreatment with endothelin-1 (ET-1) for 20 min stimulates GLUT4 translocation in a PI3-kinase dependent manner in 3T3-L1 adipocytes ( Imamura, T. et al., J Biol Chem 274 : 33691-33695 )
Janez et al., Endocrinology 2000 (Insulin Resistance) : In addition, we found that chronic insulin treatment inhibited both insulin- and osmotic shock induced membrane ruffling, indicating that two PI 3-kinase dependent effects, GLUT4 translocation and membrane ruffling are decreased in chronically insulin treated cells
Harmon et al., Biochem Biophys Res Commun 2003 : Naringenin acts by inhibiting the activity of phosphoinositide 3-kinase (PI3K) , a key regulator of insulin induced GLUT4 translocation
Nolte et al., Diabetes 2003 : Stimulation of glucose transport and GLUT4 translocation by bpV ( phen ) was completely blocked by the phosphatidylinositol 3-kinase (PI 3-K) inhibitors wortmannin and LY294002
Roberts et al., Biol Reprod 2004 : Finally, inhibition of FSH stimulated glucose uptake by the PI3-kinase inhibitor LY294002 and the finding of GLUT4 protein in granulosa cells suggest that FSH increases glucose uptake by PI3-kinase mediated translocation of GLUT4 to the granulosa cell membrane
Harmon et al., Breast Cancer Res Treat 2004 (Breast Neoplasms) : Our findings indicate that naringenin inhibits the activity of phosphoinositide 3-kinase (PI3K) , a key regulator of insulin induced GLUT4 translocation, as shown by impaired phosphorylation of the downstream signaling molecule Akt
Vijayakumar et al., Br J Pharmacol 2005 (Diabetes Mellitus, Experimental) : These effects of FSE on GLUT4 translocation and glucose uptake were inhibited by wortmannin, a phosphatidylinositol 3-kinase (PI3-K) inhibitor, and bisindolylmaleimide 1, a protein kinase C ( PKC ) -specific inhibitor
Bertola et al., J Biol Chem 2007 (Insulin Resistance) : We show here that in 3T3-L1 adipocytes HGF stimulates the phosphatidylinositol (PI) 3-kinase dependent protein kinase B (PKB) activity, AS160 phosphorylation, Glut4 translocation, and consequently, glucose uptake
Grillo et al., Brain Res 2009 : Insulin stimulated translocation of GLUT4 to the plasma membrane in rat hippocampus is PI3-kinase dependent
Lee et al., J Ethnopharmacol 2009 : CO-1 and CO-2 stimulated GLUT4 translocation are reduced by phosphatidylinositol-3-kinase (PI3-K) inhibitor
Isakoff et al., Proc Natl Acad Sci U S A 1995 : These findings indicate that activation of PI3-kinase is not sufficient to stimulate GLUT4 translocation to the plasma membrane
Kotani et al., Biochem Biophys Res Commun 1995 : These observations indicate that PI 3-kinase is necessary for insulin induced GLUT4 translocation and glucose transport in adipocytes
Evans et al., Cell Signal 1995 (Liver Neoplasms, Experimental) : We conclude that PI 3-kinase activation is necessary for maximum insulin stimulated glucose transport, translocation of GLUT4 , antilipolysis and DNA synthesis
Tanti et al., J Biol Chem 1996 : We have investigated whether PI 3-kinase activation is sufficient to promote Glut 4 translocation in transiently transfected adipocytes ... This could suggest that a specific localization of PI 3-kinase in this compartment is required for the action on Glut 4 ... Taken together, our results indicate that Glut 4 translocation can be efficiently promoted by an active form of PI 3-kinase but not by the activation of the MAP kinase pathway
Anai et al., J Biol Chem 1998 (Insulin Resistance) : The different cellular localizations of IRS proteins may account for the mechanism of insulin resistance induced by a high fat diet, considering that PI 3-kinase activation in the LDM fraction is reportedly essential for the translocation of GLUT4 in adipocytes
Valverde et al., Biochem J 1999 : Inhibition of phosphoinositide (PI) 3-kinase activity with chemical agents such as wortmannin or LY294002 partially blocked insulin induced GLUT4 mRNA accumulation, insulin induced GLUT4 protein content, GLUT4-CAT transactivation and glucose uptake