JT Treebak, S Glund, A Deshmukh, DK Klein, … - Diabetes, 2006 - Am Diabetes Assoc AMP-activated protein kinase (AMPK) is a heterotrimeric protein that regulates
glucose transport mediated by cellular stress or pharmacological agonists such
as 5-aminoimidazole-4-carboxamide 1 β-d-ribonucleoside (AICAR). AS160, a ... Cited by 83 - Related articles - BL Direct - All 7 versions
HF Kramer, CA Witczak, N Fujii, N Jessen, … - Diabetes, 2006 - Am Diabetes Assoc Insulin and contraction increase GLUT4 translocation in skeletal muscle via
distinct signaling mechanisms. Akt substrate of 160 kDa (AS160) mediates
insulin-stimulated GLUT4 translocation in L6 myotubes, presumably through ... Cited by 85 - Related articles - BL Direct - All 6 versions
MD Bruss, EB Arias, GE Lienhard, GD Cartee - Diabetes, 2005 - Am Diabetes Assoc In 3T3-L1 adipocytes, insulin-stimulated GLUT4 translocation requires
phosphorylation of the protein designated Akt substrate of 160 kDa (AS160). Both
insulin and contractions activate Akt in skeletal muscle. Therefore, we ... Cited by 102 - Related articles - All 8 versions
HF Kramer, CA Witczak, EB Taylor, N Fujii, … - Journal of Biological Chemistry, 2006 - ASBMB Insulin and contraction are potent stimulators of GLUT4 translocation and
increase skeletal muscle glucose uptake. We recently identified the Rab
GTPase-activating protein (GAP) AS160 as a putative point of convergence ... Cited by 64 - Related articles - All 6 versions
A Deshmukh, VG Coffey, Z Zhong, AV Chibalin … - Diabetes, 2006 - Am Diabetes Assoc Skeletal muscle contraction stimulates multiple signaling cascades that govern a
variety of metabolic and transcriptional events. Akt/protein kinase B regulates
metabolism and growth/muscle hypertrophy, but contraction effects on this ... Cited by 44 - Related articles - BL Direct - All 5 versions
GD Cartee, JFP Wojtaszewski - Applied Physiology, Nutrition, and Metabolism, 2007 - article.pubs.nrc-cnrc.gc.ca Abstract: Insulin and exercise, the most important physiological stimuli to
increase glucose transport in skeletal muscle, trigger a redistribution of GLUT4
glucose transporter proteins from the cell interior to the cell surface, ... Cited by 26 - Related articles - Cached - BL Direct - All 4 versions
- ►jbc.org N Fujii, MF Hirshman, EM Kane, RC Ho, LE … - Journal of Biological Chemistry, 2005 - ASBMB To examine the role of AMP-activated protein kinase (AMPK) in muscle glucose
transport, we generated muscle-specific transgenic mice (TG) carrying cDNAs of
inactive 2 ( 2i TG) and 1 ( 1i TG) catalytic subunits. Extensor digitorum ... Cited by 72 - Related articles - BL Direct - All 5 versions
HKR Karlsson, JR Zierath, S Kane, A Krook, … - Diabetes, 2005 - Am Diabetes Assoc AS160 is a newly described substrate for the protein kinase Akt that links
insulin signaling and GLUT4 trafficking. In this study, we determined the
expression of and in vivo insulin action on AS160 in human skeletal muscle. ... Cited by 78 - Related articles - All 5 versions
EB Taylor, D An, HF Kramer, H Yu, NL Fujii, … - Journal of Biological Chemistry, 2008 - ASBMB The Akt substrate of 160 kDa (AS160) is phosphorylated on Akt substrate (PAS)
motifs in response to insulin and contraction in skeletal muscle, regulating
glucose uptake. Here we discovered a dissociation between AS160 protein ... Cited by 34 - Related articles - All 6 versions
G Ramm, M Larance, M Guilhaus, DE James - Journal of Biological Chemistry, 2006 - ASBMB Translocation of the insulin-regulated glucose transporter GLUT4 to the cell
surface is dependent on the phosphatidylinositol 3-kinase/Akt pathway. The
RabGAP (Rab GTPase-activating protein) AS160 (Akt substrate of 160 kDa) is ... Cited by 43 - Related articles - All 6 versions
