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 43 - Related articles - BL Direct - All 5 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 100 - Related articles - All 8 versions
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 81 - Related articles - BL Direct - All 7 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 62 - Related articles - All 6 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 84 - Related articles - BL Direct - All 6 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 77 - Related articles - All 5 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 42 - Related articles - All 6 versions
S Kane, GE Lienhard - Biochemical and Biophysical Research …, 2005 - Elsevier Recently, we described a 160 kDa protein with a Rab GTPase activating protein
domain that is phosphorylated on multiple sites by the protein kinase Akt
(designated AS160). Phosphorylation of AS160 in adipocytes is required for ... Cited by 17 - Related articles - All 4 versions
- ►endojournals.org GR Peck, S Ye, V Pham, RN Fernando, SL … - Molecular Endocrinology, 2006 - Endocrine Soc Insulin-regulated aminopeptidase (IRAP), a marker of glucose transporter 4
(GLUT4) storage vesicles (GSVs), is the only protein known to traffic with
GLUT4. In the basal state, GSVs are sequestered from the constitutively ... Cited by 34 - Related articles - BL Direct - All 3 versions
- ►physiology.org C Wilson, M Hargreaves, KF Howlett - American Journal of Physiology- Endocrinology And …, 2006 - Am Physiological Soc The subcellular localization of insulin signaling proteins is altered by various
stimuli such as insulin, insulin-like growth factor I, and oxidative stress and
is thought to be an important mechanism that can influence intracellular ... Cited by 15 - Related articles - BL Direct - All 5 versions
