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AKT1 — INPPL1
Pathways - manually collected, often from reviews:
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 ... 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 ... 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
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
Zhang et al., Cell Signal 2007
:
SHIP2 controls PtdIns ( 3,4,5 ) P ( 3 ) levels and
PKB activity in response to oxidative stress
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