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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

TBC1 domain family, member 4

AS160, TBC1D4, Akt substrate of 160 kDa
Top mentioned proteins: Insulin, Akt, AMPK, Rab5, V1a
Papers using AS160 antibodies
A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain.
Sethi Jaswinder K., In PLoS ONE, 2001
... Akt, phospho-Akt (T308 and S473), AMPK, phospho-AMPK, and phosphotyrosine from Cell Signaling Technology (Danvers, MA), anti-AS160 from AbCam (Cambridge, MA), and anti-phospho-AS160, ...
Papers on AS160
The Effects of AS160 Modulation on Fatty Acid Transporters Expression and Lipid Profile in L6 Myotubes.
Chabowski et al., Poland. In Cell Physiol Biochem, Feb 2016
BACKGROUND/AIMS: AS160 is a key intracellular regulator of energy utilization in cells.
Mechanisms for greater insulin-stimulated glucose uptake in normal and insulin-resistant skeletal muscle after acute exercise.
Cartee, Ann Arbor, United States. In Am J Physiol Endocrinol Metab, Jan 2016
Regarding potential mediators in both normal and insulin-resistant individuals, elevated postexercise ISGU with a physiological insulin dose coincides with greater Akt substrate of 160 kDa (AS160) phosphorylation without improved proximal insulin signaling at steps from insulin receptor binding to Akt activity.
PEDF attenuates insulin-dependent molecular pathways of glucose homeostasis in skeletal myocytes.
Dass et al., Australia. In Mol Cell Endocrinol, Jan 2016
PEDF turned off both the molecular switches of GLUT4 translocation: IRS-Akt/PKB-AS160 mediated and IR-pCbl-dependent GLUT4 translocation (the molecular axis of glucose uptake).
Quercetin oppositely regulates insulin-mediated glucose disposal in skeletal muscle under normal and inflammatory conditions: The dual roles of AMPK activation.
Qi et al., Nanjing, China. In Mol Nutr Food Res, Jan 2016
METHODS AND RESULTS: Under normal conditions, quercetin impaired glucose and insulin tolerance and it attenuated insulin-mediated phosphorylation of AS160 and TBC1D1 without affecting Akt activity in male ICR mice.
Rab GAPs AS160 and Tbc1d1 play non-redundant roles in the regulation of glucose and energy homeostasis in mice.
Keller et al., Virginia, South Africa. In Am J Physiol Endocrinol Metab, Jan 2016
UNASSIGNED: The related Rab GTPase-activating proteins (Rab GAPs) AS160 and Tbc1d1 regulate the trafficking of the glucose transporter GLUT4 that controls glucose uptake in muscle and fat cells and glucose homeostasis.
Roles of TBC1D1 and TBC1D4 in insulin- and exercise-stimulated glucose transport of skeletal muscle.
Cartee, Ann Arbor, United States. In Diabetologia, 2015
This review focuses on two paralogue Rab GTPase activating proteins known as TBC1D1 Tre-2/BUB2/cdc 1 domain family (TBC1D) 1 and TBC1D4 (also called Akt Substrate of 160 kDa, AS160) and their roles in controlling skeletal muscle glucose transport in response to the independent and combined effects of insulin and exercise.
Diabetes Alters the Expression and Translocation of the Insulin-Sensitive Glucose Transporters 4 and 8 in the Atria.
Lacombe et al., Oklahoma City, United States. In Plos One, 2014
Upon insulin stimulation, we reported an increase in Akt (Th308 and s473 sites) and AS160 phosphorylation, which was positively (P<0.05)
A common Greenlandic TBC1D4 variant confers muscle insulin resistance and type 2 diabetes.
Hansen et al., Copenhagen, Denmark. In Nature, 2014
Using array-based genotyping and exome sequencing, we discovered a nonsense p.Arg684Ter variant (in which arginine is replaced by a termination codon) in the gene TBC1D4 with an allele frequency of 17%.
Metabolism and insulin signaling in common metabolic disorders and inherited insulin resistance.
Højlund, Odense, Denmark. In Dan Med J, 2014
Insulin in physiological concentrations stimulates glucose uptake in human skeletal muscle in vivo by activation of the insulin signaling cascade to glucose transport through the enzymes IRS1, PI3K, Akt2, AS160/TBC1D4 and RAC1, and to glycogen synthesis through Akt2, inhibition of GSK3 and activation of glycogen synthase (GS) via dephosphorylation of serine residues in both the NH2-terminal (site 2+2a) and the COOH-terminal end (site 3a+3b).
ATP signaling in skeletal muscle: from fiber plasticity to regulation of metabolism.
Jaimovich et al., Santiago, Chile. In Exerc Sport Sci Rev, 2014
Tetanic electrical stimulation releases adenosine triphosphate (ATP) from muscle fibers through pannexin-1 channels in a frequency-dependent manner; extracellular ATP activates signals that ultimately regulate gene expression and is able to increase glucose transport through activation of P2Y receptors, phosphatidylinositol 3-kinase, Akt, and AS160.
Mechanisms in exercise-induced increase in glucose disposal in skeletal muscle.
Goyaram et al., Cape Town, South Africa. In Med Sport Sci, 2013
Evidence is provided that these signaling pathways converge with the insulin signaling cascade at: (a) aPKC (atypical protein kinase C), which signals via GTPases to remodel microtubules along which GLUT4-containing vesicles translocate, and (b) AS160 (a 160-kDa Akt substrate that has Rab-GTPase activity) to activate microtubule motor kinesin proteins that power vesicle translocation.
The association of ClipR-59 protein with AS160 modulates AS160 protein phosphorylation and adipocyte Glut4 protein membrane translocation.
Du et al., Boston, United States. In J Biol Chem, 2012
Because ClipR-59 also interacts with Akt and enhances the interaction between Akt and AS160, we suggest that ClipR-59 functions as a scaffold protein to facilitate Akt-mediated AS160 phosphorylation, thereby regulating glucose transport
Immunofluorescent localization of the Rab-GAP protein TBC1D4 (AS160) in mouse kidney.
Loffing et al., Zürich, Switzerland. In Histochem Cell Biol, 2012
TBC1D4 may play an important role for the control of renal ion and water handling and hence for the control of extracellular fluid homeostasis.
Thr649Ala-AS160 knock-in mutation does not impair contraction/AICAR-induced glucose transport in mouse muscle.
Chen et al., Dundee, United Kingdom. In Am J Physiol Endocrinol Metab, 2012
In this study both PAS and Thr649 phosphorylation of immunoprecipitated AS160 were slightly decreased in various mouse skeletal muscle types upon in situ contraction or AICAR stimulation.
Insulin and AMPK regulate FA translocase/CD36 plasma membrane recruitment in cardiomyocytes via Rab GAP AS160 and Rab8a Rab GTPase.
Stahl et al., Saint Louis, United States. In J Lipid Res, 2012
AS160 and Rab8a regulate membrane recruitment of CD36.
Leptin reduces the expression and increases the phosphorylation of the negative regulators of GLUT4 traffic TBC1D1 and TBC1D4 in muscle of ob/ob mice.
Frühbeck et al., Pamplona, Spain. In Plos One, 2011
Leptin enhances the intracellular GLUT4 transport in skeletal muscle of ob/ob animals by reducing the expression and activity of the negative regulators of GLUT4 traffic TBC1D1 and TBC1D4.
Regulation of glucose transporter translocation in health and diabetes.
Bogan, New Haven, United States. In Annu Rev Biochem, 2011
Insulin signals through AS160/Tbc1D4 and Tbc1D1 to modulate Rab GTPases and through the Rho GTPase TC10α to act on other targets.
Mice with AS160/TBC1D4-Thr649Ala knockin mutation are glucose intolerant with reduced insulin sensitivity and altered GLUT4 trafficking.
Sakamoto et al., Dundee, United Kingdom. In Cell Metab, 2011
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.
A negative regulatory pathway of GLUT4 trafficking in adipocyte: new function of RIP140 in the cytoplasm via AS160.
Wei et al., Minneapolis, United States. In Cell Metab, 2009
Cytoplasmic RIP140 interacts with the Akt substrate AS160, thereby impeding AS160 phosphorylation by Akt; this in turn reduces GLUT4 trafficking.
Tbc1d1 mutation in lean mouse strain confers leanness and protects from diet-induced obesity.
Al-Hasani et al., Potsdam, Germany. In Nat Genet, 2008
TBC1D1, which has been recently linked to human obesity, is related to the insulin signaling protein AS160 and is predominantly expressed in skeletal muscle.
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