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AKT1 — SLC2A4
Pathways - manually collected, often from reviews:
Text-mined interactions from Literome
Bandyopadhyay et al., Mol Endocrinol 1999
:
In contrast to the T410A PKC-zeta mutant, an analogous double mutant of
PKB ( T308A/S473A ) that is resistant to PDK-1 activation had only a small effect on insulin stimulated HA-GLUT4 translocation and did not
inhibit HA-GLUT4 translocation induced by overexpression of wild-type PDK-1
Noda et al., J Med Invest 2000
:
Overexpression of wild-type
Akt1 promoted insulin stimulated p70S6 kinase (p70S6K) activity and affected GSK3 beta regulation, but did not
promote insulin stimulated
GLUT4 translocation or glucose transport in L6 myotubes ... One of the down stream effectors of PI3-kinase is serine-threonine kinase Akt ( protein kinase B, RAK-PK ), but the
involvement of
Akt in insulin stimulated
GLUT4 translocation is controversial ... To investigate whether
Akt1 regulates insulin stimulated
GLUT4 translocation and glucose uptake in L6 myotubes, we established L6 myotubes stably expressing c-myc epitope tagged GLUT4 ( GLUT4myc ) and mouse wild type ( WT ) Akt1 ... We found that overexpression of WT
Akt1 promoted insulin stimulated p70S6 kinase (p70S6K) activity and increased the basal activity of GSK3 beta, but did not
promote insulin stimulated
GLUT4 translocation or glucose uptake
Hernandez et al., FEBS Lett 2001
:
Akt mediates insulin induction of glucose uptake and up-regulation of
GLUT4 gene expression in brown adipocytes
Cormont et al., Biochem J 2001
:
Expression of a prenylation-deficient Rab4 inhibits the
GLUT4 translocation
induced by active phosphatidylinositol 3-kinase and
protein kinase B ... Rab4 DeltaCT was then shown to prevent
GLUT4 translocation
induced by the expression of an active form of phosphatidylinositol 3-kinase or of
protein kinase B , without altering the activities of the enzymes
Huisamen et al., Mol Cell Biochem 2001
(Diabetes Mellitus...) :
Glucose uptake,
glut 4 translocation and
activation of
protein kinase B were measured in Langendorff perfused hearts from ( i ) Wistar control, ( ii ) lean, neonatal Streptozotocin induced (Stz) and ( iii ) Zucker ( fa/fa ) obese diabetic rats of 10-12 weeks old
Katome et al., J Biol Chem 2003
:
We confirmed that expression of a constitutively active
Akt , using an adenoviral expression vector,
promoted translocation of
glucose transporter 4 (GLUT4) to plasma membrane, 2-deoxyglucose ( 2-DG ) uptake, and glycogen synthesis in both Chinese hamster ovary cells and 3T3-L1 adipocytes ... Inhibition of
Akt either by adenoviral expression of a dominant negative Akt or by the introduction of synthetic 21-mer short interference RNA against Akt markedly
reduced insulin stimulated
GLUT4 translocation, 2-DG uptake, and glycogen synthesis
Park et al., Diabetes 2005
(Heart Diseases...) :
Insulin stimulated cardiac glucose metabolism was significantly reduced after 1.5 weeks of high-fat feeding, and cardiac insulin resistance was associated with blunted
Akt mediated insulin signaling and
GLUT4 levels
Palmada et al., Diabetes 2006
:
The effect on
GLUT4 but not on GLUT1 is
mediated by activation of
protein kinase B (PKB)
Florholmen et al., Diabetologia 2006
(Insulin Resistance) :
Chronic LIF treatment induced insulin resistance, possibly
mediated by altered expression of Socs3 and
Slc2a4 , and impaired insulin mediated phosphorylation of GSK-3 and
Akt/PKB ... Chronic LIF treatment induced insulin resistance, possibly
mediated by altered expression of Socs3 and
Slc2a4 , and impaired insulin mediated phosphorylation of GSK-3 and
Akt/PKB
Wei et al., J Biol Chem 2006
:
Furthermore, Ang II abolished insulin induced tyrosine phosphorylation of insulin receptor substrate 1 (IRS1),
activation of
protein kinase B ( Akt ), and
glucose transporter-4 (GLUT4) translocation to the plasma membrane, which was reversed by pretreating myotubes with losartan or apocynin
Koneru et al., Am J Physiol Heart Circ Physiol 2007
(Myocardial Infarction) :
It clearly documents a significant role of ROS signaling in
Akt/eNOS/Cav-3 mediated
GLUT-4 translocation and association in IP myocardium
Saito et al., J Biol Chem 2007
:
The interaction of
Akt with APPL1 is
required for insulin stimulated
Glut4 translocation
Sano et al., Biochem J 2008
:
Previous studies have indicated that
Akt [ also known as PKB ( protein kinase B ) ] phosphorylation of AS160, a GAP ( GTPase activating protein ) for Rabs, is
required for
GLUT4 translocation
Ni et al., Proc Natl Acad Sci U S A 2007
(Insulin Resistance) :
Importantly, FoxO mediated increases in
Akt activity diminish insulin signaling, as manifested by reduced Akt phosphorylation,
reduced membrane translocation of
Glut4 , and decreased insulin triggered glucose uptake
Motaghedi et al., Obesity (Silver Spring) 2008
(Insulin Resistance) :
These data provide a functional and molecular link between the CB1 receptor and insulin sensitivity, because insulin stimulated phosphorylation of
Akt is
required for
GLUT4 translocation to the PM
Kleiman et al., Biochem Biophys Res Commun 2009
:
PKCbetaII
regulates GLUT4 translocation by regulating
Akt phosphorylation and thus activity
Tan et al., Biochem J 2011
:
We report that MK-2206 potently inhibits Thr308Akt and
Ser473Akt phosphorylation in 3T3-L1 adipocytes ( IC50 0.11 and 0.18 µM respectively ) as well as downstream
effects of insulin on
GLUT4 ( glucose transporter 4 ) translocation ( IC50 0.47 µM ) and glucose transport ( IC50 0.14 µM )
Manna et al., J Biol Chem 2011
:
Treatment with LC, H ( 2 ) S, or PIP3 increased the phosphorylation of IRS1,
AKT , and PKC?/? as well as
GLUT4 activation and glucose utilization in HG-treated cells
Nazari et al., Biochemistry (Mosc) 2011
:
Conversely, cortactin mutants lacking the Src homology 3 (SH3) domain inhibited insulin stimulated formation of actin stress fibers and
GLUT4 translocation similar to the actin depolymerizing agent cytochalasin D. Wortmannin, genistein, and a PP1 analog completely
blocked insulin induced
Akt phosphorylation, formation of actin stress fibers, and GLUT4 translocation indicating the involvement of both PI3-K/Akt and the Src family of kinases
Ijuin et al., J Biol Chem 2012
:
Insulin induced translocation of
GLUT4 to the plasma membrane
requires phosphatidylinositol 3-kinase activation mediated generation of phosphatidylinositol 3,4,5-trisphosphate PIP ( 3 ) and subsequent activation of
Akt
Rodríguez-Jimnez et al., Stem Cells 2012
(Spinal Cord Injuries) :
Here we show that phosphorylation of
AKT and AMP activated kinase (AMPK) is
involved in FM19G11 dependent activation of
GLUT-4 , glucose influx, and consequently in stem cell self-renewal
Miegueu et al., Am J Physiol Gastrointest Liver Physiol 2013
:
These SP effects were accompanied by downregulation of insulin receptor substrate 1 ( -82 ± 2 %, P < 0.01 ) and
GLUT4 ( -76 ± 2 %, P < 0.01 ) mRNA expression, and SP acutely
blocked insulin mediated stimulation of fatty acid uptake and
Akt phosphorylation
Dalla-Riva et al., J Lipid Res 2013
:
A survey of domain-specific peptides of apoA-I showed that the lipid-free C-terminal 190-243 fragment increases plasma membrane
GLUT4 , promotes glucose uptake, and
activates AMPK signaling but not
Akt
Nozaki et al., Cell Signal 2013
:
Insulin induced, but not constitutively activated Rac1 induced,
GLUT4 translocation was
suppressed by
Akt inhibitor IV
Meng et al., Journal of diabetes research 2013
:
Meanwhile, the insulin signaling was markedly increased as shown by increased phosphorylation of
Akt and enhanced
GLUT4 activation
Ji et al., PloS one 2013
:
Moreover, the PI3K inhibitor wortmannin significantly inhibited
activation of
Akt and AMPK, reduced
GLUT4 translocation, glucose uptake and ultimately, depressed IPC induced cardioprotection
Cong et al., Mol Endocrinol 1997
:
Physiological
role of
Akt in insulin stimulated translocation of
GLUT4 in transfected rat adipose cells ... Overexpression of
Akt-WT resulted in significant translocation of
GLUT4 to the cell surface even in the absence of insulin ... More importantly, overexpression of
Akt-K179A ( kinase-inactive mutant ) significantly
inhibited insulin stimulated translocation of
GLUT4
Kotani et al., Mol Cell Biol 1998
:
A PKClambda mutant that lacks the pseudosubstrate domain ( lambdaDeltaPD ) exhibited markedly increased kinase activity relative to that of the wild-type enzyme, and expression of lambdaDeltaPD in quiescent 3T3-L1 adipocytes resulted in the stimulation of glucose uptake and translocation of
GLUT4 but not in the
activation of
Akt