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AKT1 — GYS1

Text-mined interactions from Literome

Filippa et al., Mol Cell Biol 1999 : We looked at events downstream of PKB and found that PKA activation of PKB led to the phosphorylation and inhibition of glycogen synthase kinase-3 ( GSK-3 ) activity, a known in vivo substrate of PKB
Takata et al., J Biol Chem 1999 : Requirement for Akt ( protein kinase B ) in insulin induced activation of glycogen synthase and phosphorylation of 4E-BP1 ( PHAS-1 ) ... The roles of Akt ( protein kinase B ) and the atypical lambda isoform of protein kinase C ( PKClambda ), both of which act downstream of phosphoinositide 3-kinase, in the activation of glycogen synthase and phosphorylation of 4E-BP1 ( PHAS-1 ) in response to insulin were investigated ... A mutant Akt ( Akt-AA ) in which the phosphorylation sites targeted by growth factors are replaced by alanine was shown to inhibit insulin induced activation of both Akt and glycogen synthase in L6 myotubes ... Expression of a mutant Akt in which Lys179 in the kinase domain was replaced by aspartate also inhibited insulin induced activation of glycogen synthase but had no effect on insulin activation of endogenous Akt ... These data suggest that Akt , but not PKClambda, is required for insulin activation of glycogen synthase and for insulin induced phosphorylation of 4E-BP1
Troussard et al., Mol Cell Biol 1999 : ILK activates protein kinase B and inhibits the glycogen synthase kinase 3 ( GSK-3 ) activity in a phosphatidylinositol-3-kinase ( PI 3-kinase ) -dependent manner
Egawa et al., Endocrinology 2000 (Insulin Resistance) : Recently, we have reported that the overexpression of a membrane targeted phosphatidylinositol (PI) 3-kinase ( p110CAAX ) stimulated p70S6 kinase, Akt , glucose transport, and Ras activation in the absence of insulin but inhibited insulin stimulated glycogen synthase activation and MAP kinase phosphorylation in 3T3-L1 adipocytes
Syed et al., Mol Cell Biochem 2000 : These data suggest that stimulation of glycogen synthase by insulin in HepG2 cells is mediated through the PI-3 kinase pathway by activating PKB and PP-1G and inactivating GSK-3beta
Rössig et al., J Biol Chem 2002 : In various cell types, AKT phosphorylates and inhibits glycogen synthase kinase-3 ( GSK-3 )
Sakoda et al., J Biol Chem 2003 (Cell Transformation, Neoplastic...) : We found that adenovirus mediated overexpression of myristoylated ( myr- ) forms of Akt resulted in high glucose transport activity in 3T3-L1 adipocytes, phosphorylated glycogen synthase kinase-3 ( GSK3 ) and enhanced glycogen synthase activity in hepatocytes, and the promotion of DNA synthesis in interleukin-3 dependent 32D cells
Seminario et al., Eur J Immunol 2004 : The effect of PTEN on distal TCR signaling events was strongly correlated with the loss of the constitutive Akt activation and glycogen synthase kinase-3 ( GSK3 ) inhibition that is typical of Jurkat cells, and could be reversed by expression of activated Akt or pharmacologic inhibition of GSK3
González et al., Regul Pept 2005 : In rat hepatocytes, activation of PI3K/PKB , PKC and PP-1 mediates the GLP-1 induced stimulation of glycogen synthase
Aiston et al., Diabetologia 2006 : This is explained by a pathway downstream of PKB leading to inactivation of phosphorylase, activation of glycogen synthase , and stimulation of glycogen synthesis, independent of the GSK-3 pathway
Shen et al., Exp Cell Res 2006 (Breast Neoplasms) : PTHrP expression also increased the levels of phosphorylated Akt , with a consequent increase in the levels of phosphorylated ( inactive ) glycogen synthase kinase-3 ( GSK-3 )
Bodine et al., Med Sci Sports Exerc 2006 : Recent work in mammals has suggested that activation of Akt/PKB , a Ser-Thr phosphatidylinositol regulated kinase, and its downstream targets, glycogen synthase kinase-3 ( GSK3 ) and the mammalian target of rapamycin (mTOR), may be critical regulators of postnatal cell size in multiple organ systems, including skeletal muscle ... Recent work in mammals has suggested that activation of Akt/PKB , a Ser-Thr phosphatidylinositol regulated kinase, and its downstream targets, glycogen synthase kinase-3 ( GSK3 ) and the mammalian target of rapamycin (mTOR), may be critical regulators of postnatal cell size in multiple organ systems, including skeletal muscle
Kumar et al., Mol Cell Biol 2008 : However, the phosphorylation of Akt at Thr308 was normal and sufficient to mediate the phosphorylation of glycogen synthase kinase 3 ( GSK-3 )
Wang et al., J Surg Res 2009 (Breast Neoplasms) : Moreover, a combination of TZDs and a specific Akt inhibitor may serve as a new approach to target Wnt/beta-catenin directly and via PI3K/Akt action on glycogen synthase-3beta
Li et al., Neurobiol Aging 2012 (Alzheimer Disease...) : In SK-NS-H cells, upregulation of AGEs receptor ( RAGE ), inhibition of Akt , and activation of glycogen synthase kinase-3 ( GSK-3 ) , Erk1/2, and p38 were observed after treatment with AGEs
Oviedo-Boyso et al., Infect Immun 2011 : Furthermore, Akt activation by internalized S. aureus triggered a time dependent phosphorylation of glycogen synthase kinase-3a ( GSK-3a ) on Ser21 and GSK-3ß on Ser9 that was partially inhibited with SH-5
Sen et al., Stem Cells 2011 : The suppression of MSC adipogenesis by mechanical stimuli, which requires Akt induced inhibition of glycogen synthase kinase 3ß ( GSK3ß ) with ß-catenin activation, can be enhanced by repetitive dosing within a single day
Wang et al., J Cell Biochem 2012 : We showed that IL-6 activated Akt and inhibited glycogen synthase kinase-3ß ( GSK-3ß ) , highly associating with fascin-1 mRNA expression
Chen et al., Neuroendocrinology 2013 : Results : In Hcy treated SH-SY5Y cells, E2 increased cell viability, attenuated ROS production, activated Akt signaling and inhibited glycogen synthase kinase-3ß ( GSK-3ß ) , a kinase known to participate in neurodegeneration
Abushahba et al., PloS one 2012 (Melanoma) : In the present study, we demonstrate that riluzole inhibits AKT mediated glycogen synthase kinase 3 ( GSK3 ) phosphorylation in melanoma cell lines
Wang et al., Toxicol Lett 2013 (Glioma) : In mechanisms, we verified that wogonin significantly diminished the phosphorylated level of protein kinase B ( AKT ), and maintenance of low ß-catenin expression level was dependent on glycogen synthase kinase 3ß ( GSK3ß ) activation at Ser9 ... In mechanisms, we verified that wogonin significantly diminished the phosphorylated level of protein kinase B ( AKT ), and maintenance of low ß-catenin expression level was dependent on glycogen synthase kinase 3ß ( GSK3ß ) activation at Ser9
Hurel et al., Biochem J 1996 : Insulin also causes inactivation of glycogen synthase kinase-3 ( GSK-3 ) and activation of protein kinase B , both processes being sufficiently rapid to account for the effects of insulin on GS
van Weeren et al., J Biol Chem 1998 : Activation of phosphatidylinositide 3'-OH kinase ( PI 3-kinase ) is implicated in mediating a variety of growth factor induced responses, among which are the inactivation of glycogen synthase kinase-3 ( GSK-3 ) and the activation of the serine/threonine protein kinase B (PKB)
Dandekar et al., Endocrinology 1998 : The cytoplasmic domain of the IRR was found to 1 ) mediate activation of the Ser/Thr kinase Akt/PKB , 2 ) stimulate glucose uptake, 3 ) inhibit lipolysis, and 4 ) stimulate glycogen synthase , all with a potency comparable to those of the expressed CSF-1R/IR chimera and the endogenous insulin receptors ... The cytoplasmic domain of the IRR was found to 1 ) mediate activation of the Ser/Thr kinase Akt/PKB , 2 ) stimulate glucose uptake, 3 ) inhibit lipolysis, and 4 ) stimulate glycogen synthase , all with a potency comparable to those of the expressed CSF-1R/IR chimera and the endogenous insulin receptors