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AKT2 — INPPL1

Text-mined interactions from Literome

Ishihara et al., Biochem Biophys Res Commun 1999 : Interestingly, although both PtdIns- ( 3,4,5 ) P3 and PtdIns ( 3,4 ) P2 have been implicated in the regulation of Akt activity in vitro, overexpression of SHIP2 inhibited insulin induced Akt activation, presumably by its 5'-inositol phosphatase activity
Blero et al., Biochem Biophys Res Commun 2001 : Overexpression of SHIP2 led to a decrease of the insulin dependent PIP3 production as well as Akt/PKB activation and MAPK stimulation
Sasaoka et al., Diabetologia 2001 : Although PI ( 3,4,5 ) P3 and PI ( 3,4 ) P2 are known to possibly activate a downstream molecule of PI3-kinase Akt in vitro, overexpression of WT-SHIP2 inhibited insulin induced phosphorylation and activation of Akt
Choi et al., Oncogene 2002 (MAP Kinase Signaling System...) : Although SHIP2 expression resulted in suppression of interleukin-6 mediated mitogen activated protein kinase activation, expression of SHIP and SHIP2 in a PTEN-null myeloma line did not suppress Akt activity
Ishihara et al., Mol Endocrinol 2002 : We investigated the molecular mechanism by which SHIP2 negatively regulates insulin induced phosphorylation of Akt , a key downstream molecule of phosphatidylinositol 3-kinase important for the biological action of insulin ... Overexpression of wild-type SHIP2 ( WT-SHIP2 ) inhibited insulin induced phosphorylation of Akt at both Thr ( 308 ) and Ser ( 473 ) in Rat1 fibroblasts expressing insulin receptors ... These results indicate that the membrane localization of SHIP2 with its 5'-phosphatase activity is required for negative regulation of insulin induced Akt phosphorylation and that the localization is regulated, at least in part, by the association of SHIP2 with Shc in Rat1 fibroblasts
Pengal et al., J Biol Chem 2003 : Furthermore, FcgammaRIIa induced Akt activation was blocked by wild-type SHIP-2 , but not by a catalytically deficient mutant of SHIP-2
Sasaoka et al., J Biol Chem 2004 : Insulin induced phosphorylation of Akt , one of the molecules downstream of PI3-kinase, was inhibited by expression of wild-type SHIP2 , whereas it was increased by expression of 5'-phosphatase-defective ( DeltaIP ) SHIP2 in whole cell lysates ... Thus, insulin induced phosphorylation of Akt2 at the PM was predominantly regulated by SHIP2 , whereas the phosphorylation of Akt1 was only minimally affected ... Although the expression of a constitutively active form of PI3-kinase myr-p110 also elicited a subcellular redistribution of SHIP2 to the PM, expression of SHIP2 appeared to affect the myr-p110 induced phosphorylation, and not the translocation, of Akt2 ... Furthermore, insulin induced phosphorylation of Akt was effectively regulated by SHIP2 in embryonic fibroblasts derived from knockout mice lacking either insulin receptor substrate-1 or insulin receptor substrate-2
Kagawa et al., J Clin Endocrinol Metab 2005 : Transfection study showed that expression of SNP3-SHIP2 inhibited insulin induced PI ( 3,4,5 ) P3 production and Akt2 phosphorylation less potently than expression of wild-type SHIP2 in CHO-IR cells
Grempler et al., Diabetes 2007 : Liver-specific expression of a dominant negative SHIP2 mutant in KKA ( y ) mice increased basal and insulin stimulated Akt phosphorylation
Grempler et al., FEBS Lett 2007 (Insulinoma) : Here we show that SHIP2 inhibition in INS1E insulinoma cells increased Akt , glycogen synthase kinase 3 and extracellular signal regulated kinases 1 and 2 phosphorylation
Prasad et al., Int J Oncol 2009 (Breast Neoplasms) : These results demonstrate a positive role of SHIP2 in EGF induced Akt activation, CXCR4 expression, and cell migration in breast cancer cells
Hyvönen et al., Mol Cell Endocrinol 2010 (Proteinuria) : Overexpression of SHIP2 in cultured podocytes reduces Akt activation in response to insulin, and promotes apoptosis