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INS — TBC1D4

Text-mined interactions from Literome

Sano et al., J Biol Chem 2003 : These findings strongly indicate that insulin stimulated phosphorylation of AS160 is required for GLUT4 translocation and that this phosphorylation signals translocation through inactivation of the Rab GAP function
Zeigerer et al., Mol Biol Cell 2004 : Insulin stimulation of GLUT4 exocytosis, but not its inhibition of endocytosis, is dependent on RabGAP AS160
Bruss et al., Diabetes 2005 : Increased phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle in response to insulin or contractile activity
Karlsson et al., Diabetes 2005 (Diabetes Mellitus, Type 2) : Insulin increased insulin receptor substrate 1 (IRS-1) tyrosine phosphorylation, IRS-1 associated phosphatidylinositol (PI) 3-kinase activity, and phosphorylation of Akt Ser473 and AS160 , a newly described Akt substrate that plays a role in GLUT4 exocytosis, approximately 2.3 fold before treatment
Karlsson et al., Diabetes 2005 (Diabetes Mellitus, Type 2) : Insulin stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects ... In this study, we determined the expression of and in vivo insulin action on AS160 in human skeletal muscle ... Insulin stimulated AS160 phosphorylation was reduced 39 % ( P < 0.05 ) in type 2 diabetic patients ... Moreover, defects in insulin action on AS160 may impair GLUT4 trafficking in type 2 diabetes
Karlsson et al., Diabetes 2006 (Diabetes Mellitus, Type 2) : Insulin increased phosphorylation of Akt and Akt substrate of 160 kDa (AS160) in a dose dependent manner, with comparable responses between groups
Kramer et al., Diabetes 2006 : Distinct signals regulate AS160 phosphorylation in response to insulin , AICAR, and contraction in mouse skeletal muscle ... Using in vivo, in vitro, and in situ methods, insulin , contraction, and the AMP activated protein kinase (AMPK) activator AICAR all increased AS160 phosphorylation in mouse skeletal muscle ... Insulin stimulated AS160 phosphorylation was fully blunted by wortmannin in vitro and in Akt2 knockout ( KO ) mice in vivo ... Maximal insulin , together with either AICAR or contraction, increased AS160 phosphorylation in an additive manner
Ramm et al., J Biol Chem 2006 : These data show that the insulin dependent association of 14-3-3 with AS160 plays an important role in GLUT4 trafficking in adipocytes
Kramer et al., J Biol Chem 2006 : To determine the effects of AS160 on insulin- and contraction stimulated glucose uptake in transfected muscles, we measured [ 3H ] 2-deoxyglucose uptake in vivo following intravenous glucose administration and in situ muscle contraction, respectively
Jager et al., Endocrinology 2007 (Inflammation...) : Moreover, IRS-1 protein expression and insulin induced protein kinase B activation , AS160 phosphorylation, and Glut 4 translocation were partially recovered after treatment with the ERK inhibitor
Arias et al., Am J Physiol Endocrinol Metab 2007 : Insulin caused a significant increase in pSerAkt, pThrAkt, pGSK3, and AS160 phosphorylation with or without exercise
Thong et al., Diabetes 2007 : Insulin dependent phosphorylation of Akt target AS160 is required for GLUT4 translocation ... PDGF and insulin increased AS160 phosphorylation in CHO-IR cells
Howlett et al., Diabetes 2007 (Hyperinsulinism) : Resistance exercise and insulin regulate AS160 and interaction with 14-3-3 in human skeletal muscle ... Insulin increased ( P < 0.05 ) phosphorylation of AS160 and its interaction with 14-3-3, but the insulin response was not influenced by resistance exercise
Cartee et al., Appl Physiol Nutr Metab 2007 : Insulin also induces a rapid and dose dependent increase in AS160 phosphorylation in skeletal muscle ... AMP activated protein kinase (AMPK) is likely important for phosphorylating AS160 in response to exercise/contractile activity, whereas Akt2 appears to be important for insulin stimulated AS160 phosphorylation in muscle
Alkhateeb et al., Am J Physiol Endocrinol Metab 2007 (Insulin Resistance) : In contrast, intramuscular ceramide ( +24 % ) and diacylglycerol ( +32 % ) concentrations, insulin stimulated AS160 ( -36 % ) and PRAS40 ( -33 % ) phosphorylations, and Akt ( -40 % ), PKCtheta ( -50 % ), and GLUT4 translocation ( -40 % ) to the plasma membrane were all maximally altered within the first 6 h of palmitate treatment
Hakuno et al., J Biol Chem 2007 : Although 53BP2S also enhanced Akt activation in 3T3-L1 adipocytes, insulin induced glucose transporter 4 translocation was markedly inhibited in accordance with reduction of insulin induced AS160 phosphorylation
Kumar et al., Mol Cell Biol 2008 : Furthermore, insulin stimulated phosphorylation of the Akt substrate AS160 at Thr642 was reduced in rictor knockout muscle, indicating a defect in insulin signaling to stimulate glucose transport
Højlund et al., Diabetes 2008 (Obesity...) : Impaired insulin stimulated phosphorylation of Akt and AS160 in skeletal muscle of women with polycystic ovary syndrome is reversed by pioglitazone treatment ... Impaired insulin mediated total ( R ( d ) ) oxidative and nonoxidative glucose disposal ( NOGD ) was paralleled by reduced insulin stimulated Akt phosphorylation at Ser473 and Thr308 and AS160 phosphorylation in muscle of PCOS patients
Chen et al., Biochem J 2008 : Complementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators
Howlett et al., Am J Physiol Endocrinol Metab 2008 : The effect of exercise and insulin on AS160 phosphorylation and 14-3-3 binding capacity in human skeletal muscle ... The effects of aerobic exercise and subsequent insulin stimulation on AS160 phosphorylation and the binding capacity of 14-3-3, a novel protein involved in the dissociation of AS160 from GLUT4 vesicles, in human skeletal muscle are unknown ... Insulin increased AS160 phosphorylation and 14-3-3 binding capacity and insulin receptor substrate-1 and Akt phosphorylation, but the response to insulin was not enhanced by prior exercise ... Insulin increases AS160 phosphorylation and 14-3-3 binding capacity, but prior exercise does not appear to enhance the response to insulin
Montessuit et al., Endocrinology 2008 (Insulin Resistance) : Phosphorylation of Akt and AS160 in response to insulin was lower in insulin-resistant cardiomyocytes
Wueest et al., Diabetologia 2009 (Insulin Resistance) : Similarly, insulin stimulated phosphorylation of protein kinase B and AS160 were reduced to the same extent in small and large adipocytes isolated from HFD-mice
Wright et al., Cardiovasc Res 2009 (Disease Models, Animal...) : Insulin stimulated Akt/PKB and AS-160 phosphorylation were preserved, and PDH activity was unchanged
Funai et al., Diabetes 2009 : Insulin stimulated phosphorylation ( measured using the phospho-Akt substrate [ PAS ] antibody ) of AS160 and TBC1D1 appears to occur in an Akt dependent manner, but the kinases responsible for contraction stimulated PAS-AS160 and PAS-TBC1D1 remain unclear ... Insulin stimulated glucose transport and phosphorylation of both AS160 and TBC1D1 were completely inhibited by Wortmannin
Sharma et al., Physiol Res 2010 : Rapid reversal of insulin stimulated AS160 phosphorylation in rat skeletal muscle after insulin exposure ... The primary aim of this study was to characterize the time course for reversal of insulin stimulated AS160 phosphorylation in rat skeletal muscle after insulin removal
Treebak et al., Diabetologia 2009 (Hyperinsulinism) : However, TBC1D4 phosphorylation on Ser-318, Ser-341, Ser-588 and Ser-751 was higher in the previously exercised leg, both in the absence and in the presence of insulin ( p < 0.01 ; Ser-588, p = 0.09 ; observed power = 0.39 )
Lee et al., J Biol Chem 2009 (Diabetes Mellitus, Type 2...) : Insulin induced phosphorylation of Akt, AS160 , S6K, and S6 was also decreased in skeletal muscle
Funai et al., Am J Physiol Endocrinol Metab 2009 (Insulin Resistance) : The results indicated that, in isolated rat epitrochlearis muscle, 1 ) elevated phosphorylation of AS160 ( measured using anti-phospho-Akt substrate, PAS-AS160, and phosphospecific anti-Thr ( 642 ) -AS160, pThr ( 642 ) -AS160 ) consistently tracked with elevated insulin stimulated GT ; 2 ) PAS-TBC1D1 was not different from sedentary values at 3 or 27 h postexercise, when insulin sensitivity was increased ; 3 ) insulin stimulated Akt activity was not increased postexercise in muscles with increased insulin sensitivity ; 4 ) PAS-TBC1D1 was increased immediately postexercise, when insulin independent GT was elevated, and reversed at 3 and 27 h postexercise, when insulin independent GT was also reversed ; and 5 ) there was no significant effect of exercise or insulin on total abundance of AS160 , TBC1D1, Akt, or GLUT4 protein with any of the protocols
Pehmøller et al., Am J Physiol Endocrinol Metab 2009 : Thus, TBC1D1 is differentially regulated in response to insulin and contraction
Xie et al., Cell Res 2009 (Diabetes Mellitus, Type 2) : Depletion of RUVBL2 in adipocytes inhibits insulin stimulated GLUT4 translocation and glucose uptake through reducing insulin stimulated AS160 phosphorylation
Alkhateeb et al., Am J Physiol Endocrinol Metab 2009 (Insulin Resistance) : In contrast, palmitate oxidation and insulin stimulated AS160 phosphorylation were highly correlated ( r = 0.83 )
Bikman et al., Am J Physiol Regul Integr Comp Physiol 2010 (Insulin Resistance...) : We found that a 1-h palmitate incubation in lean myotubes reduced ( P < 0.05 ) insulin stimulated phosphoprotein kinase B ( Akt ), Akt substrate 160 (AS160) , and inhibitory factor kappaBalpha ( IkappaBalpha ) mass, all of which were prevented with AICAR inclusion
Gaidhu et al., Mol Endocrinol 2010 : Subsequently, basal and insulin stimulated glucose uptake and the phosphorylation of AMPK, acetyl-CoA carboxylase, Akt, and the Akt substrate of 160 kDa ( AS160/TBC1D4 ) were determined
Alkhateeb et al., Am J Physiol Regul Integr Comp Physiol 2010 (Insulin Resistance) : Palmitate oxidation, AMPK/acetyl-CoA carboxylase (ACC) phosphorylation and insulin stimulated glucose transport, plasmalemmal GLUT4, and AS160 phosphorylation were examined at 0, 6, and 12 h. Palmitate treatment for 12 h reduced fatty acid oxidation ( -47 % ), and insulin stimulated glucose transport ( -71 % ), GLUT4 translocation ( -40 % ), and AS160 phosphorylation ( -26 % ), but it increased AMPK ( +51 % ) and ACC phosphorylations ( +44 % ) ... Inhibition of AMPK phosphorylation with adenine 9-beta-d-arabinofuranoside (Ara) ( 2.5 mM ) or compound C ( 50 muM ) inhibited the thujone induced improvement in insulin stimulated glucose transport, GLUT4 translocation, and AS160 phosphorylation
Ching et al., Am J Physiol Cell Physiol 2010 (Starvation) : Serum starvation did not affect p38, PKC?, or AS160 phosphorylation or insulin stimulated Akt or AS160 phosphorylation
Sun et al., Proc Natl Acad Sci U S A 2010 : Constitutively active AS160 lowered basal and insulin stimulated levels of surface GLUT4, effects that were reversed by overexpressing Rab8A or Rab13, suggesting that both Rabs are targets of AS160-GAP activity in the context of GLUT4 traffic
Chen et al., Cell Metab 2011 : The mutant protein was expressed at normal levels, while insulin stimulated AS160 binding to 14-3-3s was abolished in homozygous knockin mice ... These results provide genetic evidence that insulin induced AS160-Thr649 phosphorylation and/or its binding to 14-3-3 play an important role in regulating whole-body glucose homeostasis, at least in part through regulating GLUT4 trafficking in muscle
Koumanov et al., J Biol Chem 2011 : These data suggest a model for PTB domain action on GLUT4 vesicle fusion in which these constructs inhibit insulin stimulated 14-3-3? interaction with AS160 rather than AS160 phosphorylation
Cleasby et al., J Endocrinol 2011 (Insulin Resistance) : These effects are likely explained by APPL1 OE-induced increase in basal and insulin stimulated phosphorylation of IRS1, AKT, GSK3ß and TBC1D4
Breen et al., PloS one 2011 : Basal 24 h post-RE and insulin stimulated PAS-AS160/TBC1D4 phosphorylation was greater for EX and EX+PRO
Kewalramani et al., PloS one 2011 (Inflammation...) : This palmitate-free CM-PA, containing selective cytokines and chemokines, inhibited myoblast insulin stimulated insulin receptor substrate 1 (IRS1) tyrosine phosphorylation, AS160 phosphorylation, GLUT4 translocation and glucose uptake
Samovski et al., J Lipid Res 2012 (MAP Kinase Signaling System) : Our study documents that AS160 mediates insulin or AMPK stimulated surface translocation of CD36 in cardiomyocytes
Ducommun et al., Am J Physiol Endocrinol Metab 2012 : Insulin increases AS160 phosphorylation at multiple Akt/PKB consensus sites, including Thr ( 649 ), and promotes its binding to 14-3-3 proteins through phospho-Thr ( 649 )
Li et al., Diabetes 2013 (Diabetes Mellitus, Type 2...) : In palmitate induced insulin-resistant C2C12 myotubes, telmisartan enhanced insulin stimulated Akt and Akt substrate of 160 kDa (AS160) phosphorylation as well as Glut4 translocation to the plasma membrane
Asrih et al., J Mol Cell Cardiol 2013 : In cardiomyocytes exposed to 1nM CT-1 there was also reduced phosphorylation of Akt and AS160 in response to insulin , and of AMPK in response to oligomycin ... On the other hand in cardiomyocytes exposed to 10nM CT-1 there was increased phosphorylation of the AS160 and Akt in response to insulin
Liang et al., PloS one 2013 : This inflammatory response led to reduced insulin stimulated IRS-1, Akt and AS160 phosphorylation and impaired glucose transport
Ching et al., Applied physiology, nutrition, and metabolism = Physiologie appliquée, nutrition et métabolisme 2013 : However, insulin did not stimulate glucose transport or the phosphorylation of AS160 in ATM-/- soleus
Middelbeek et al., Nutrition & diabetes 2013 : These data show that insulin differentially regulates AS160 and TBC1D1 phosphorylation in human skeletal muscle