A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain.
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, ...
Metabolism and insulin signaling in common metabolic disorders and inherited insulin resistance.
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.
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.
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.