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IRS2 — PI3

Text-mined interactions from Literome

Khan et al., Diabetes 2001 : Insulin is known to regulate pancreatic beta-cell function through the activation of cell surface insulin receptors, phosphorylation of insulin receptor substrate (IRS)-1 and -2 , and activation of phosphatidylinositol (PI) 3-kinase
Kanoh et al., Endocrinology 2003 (Diabetes Mellitus, Experimental) : Insulin induced activation of aPKCs was impaired in both high-fat fed and STZ-diabetic rats, but, surprisingly, IRS-1 dependent and IRS-2 dependent PI 3-kinase activation was not appreciably compromised
Valverde et al., Diabetes 2003 (Insulin Resistance) : The lack of IRS-2 did not result in enhanced IRS-1 tyrosine phosphorylation or IRS-1 associated phosphatidylinositol (PI) 3-kinase activity on insulin stimulation
Venieratos et al., Cell Signal 2010 : Results showed that prolonged exposure of betaTC-6 cells to increased glucose concentrations resulted in significant inhibition of insulin induced tyrosine phosphorylation of the insulin receptor (IR), and insulin receptor substrate-2 (IRS-2) as well as PI3-kinase activation
Tsunekawa et al., Diabetes 2011 : In contrast, inhibition of phosphatidylinositol 3-kinase (PI3K) or PKB significantly increased IRS-2 levels in ß-cells
Sajan et al., Diabetologia 2012 (Diabetes Mellitus, Type 2) : Heightened PKC-? activity most likely reflected heightened activity of IRS-2 dependent phosphatidylinositol 3-kinase (PI3K) , as IRS-1 levels and IRS-1/PI3K activity were markedly diminished
Neukamm et al., PloS one 2012 : Phosphorylation of insulin receptor substrate (IRS)-2 on tyrosine residues is a key event in IGF-1/insulin signaling and leads to activation of the PI 3-kinase and the Ras/MAPK pathway