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AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain

Biochemical journal, 2005-10, Vol.391 (Pt 1), p.87-93

2005

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Rab10, a Target of the AS160 Rab GAP, Is Required for Insulin-Stimulated Translocation of GLUT4 to the Adipocyte Plasma Membrane

Cell metabolism, 2007-04, Vol.5 (4), p.293-303

2007

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Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1

Biochemical journal, 2007-04, Vol.403 (2), p.353-358

2007

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Insulin-stimulated GLUT4 Protein Translocation in Adipocytes Requires the Rab10 Guanine Nucleotide Exchange Factor Dennd4C

The Journal of biological chemistry, 2011-05, Vol.286 (19), p.16541-16545

2011

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Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation

The Journal of biological chemistry, 2003-04, Vol.278 (17), p.14599-14602

2003

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Rab10 in insulin-stimulated GLUT4 translocation

Biochemical journal, 2008-04, Vol.411 (1), p.89-95

2008

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Full intracellular retention of GLUT4 requires AS160 Rab GTPase activating protein

Cell metabolism, 2005-10, Vol.2 (4), p.263-272

2005

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Increased Phosphorylation of Akt Substrate of 160 kDa (AS160) in Rat Skeletal Muscle in Response to Insulin or Contractile Activity

Diabetes (New York, N.Y.), 2005-01, Vol.54 (1), p.41-50

2005

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Inhibition of GLUT4 Translocation by Tbc1d1, a Rab GTPase-activating Protein Abundant in Skeletal Muscle, Is Partially Relieved by AMP-activated Protein Kinase Activation

The Journal of biological chemistry, 2008-04, Vol.283 (14), p.9187-9195

2008

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Insulin-Stimulated Phosphorylation of the Akt Substrate AS160 Is Impaired in Skeletal Muscle of Type 2 Diabetic Subjects

Diabetes (New York, N.Y.), 2005-06, Vol.54 (6), p.1692-1697

2005

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Temporal Dynamics of Tyrosine Phosphorylation in Insulin Signaling

Diabetes (New York, N.Y.), 2006-08, Vol.55 (8), p.2171-2179

2006

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κB-Ras Proteins Regulate Both NF-κB-Dependent Inflammation and Ral-Dependent Proliferation

Cell reports (Cambridge), 2014-09, Vol.8 (6), p.1793-1807

2014

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Non-functional phosphorylations?

Trends in biochemical sciences (Amsterdam. Regular ed.), 2008-08, Vol.33 (8), p.351-352

Lienhard, Gustav E.

2008

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Insulin-stimulated Phosphorylation of the Rab GTPase-activating Protein TBC1D1 Regulates GLUT4 Translocation

The Journal of biological chemistry, 2009-10, Vol.284 (44), p.30016-30023

2009

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A potential link between insulin signaling and GLUT4 translocation: Association of Rab10-GTP with the exocyst subunit Exoc6/6b

Biochemical and biophysical research communications, 2015-09, Vol.465 (3), p.601-605

2015

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Mice lacking insulin receptor substrate 4 exhibit mild defects in growth, reproduction, and glucose homeostasis

American journal of physiology: endocrinology and metabolism, 2000-01, Vol.278 (1), p.E127-E133

2000

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Lipoatrophic diabetes in Irs1(-/-)/Irs3(-/-) double knockout mice

Genes & development, 2002-12, Vol.16 (24), p.3213-3222

2002

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Calmodulin binds to the Rab GTPase activating protein required for insulin-stimulated GLUT4 translocation

Biochemical and biophysical research communications, 2005-09, Vol.335 (1), p.175-180

2005

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Insulin stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes

Bioscience reports, 2009-08, Vol.29 (4), p.229-235

2009

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A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain

The Journal of biological chemistry, 2002-06, Vol.277 (25), p.22115-22118

2002

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Insulin Receptor Substrate 4 Associates with the Protein IRAS

The Journal of biological chemistry, 2002-05, Vol.277 (22), p.19439-19447

2002

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SPECHT — Single-stage phosphopeptide enrichment and stable-isotope chemical tagging: Quantitative phosphoproteomics of insulin action in muscle

Journal of proteomics, 2015-01, Vol.114, p.48-60

2015

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Impact of Genetic Background and Ablation of Insulin Receptor Substrate (IRS)-3 on IRS-2 Knock-out Mice

The Journal of biological chemistry, 2003-04, Vol.278 (16), p.14284-14290

2003

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The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family

The Journal of biological chemistry, 1997-04, Vol.272 (17), p.11439-11443

1997

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Sequence and Structure of a Human Glucose Transporter

Science (American Association for the Advancement of Science), 1985-09, Vol.229 (4717), p.941-945

1985

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AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain

Rab10, a Target of the AS160 Rab GAP, Is Required for Insulin-Stimulated Translocation of GLUT4 to the Adipocyte Plasma Membrane

Substrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1

Insulin-stimulated GLUT4 Protein Translocation in Adipocytes Requires the Rab10 Guanine Nucleotide Exchange Factor Dennd4C

Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation

Rab10 in insulin-stimulated GLUT4 translocation

Full intracellular retention of GLUT4 requires AS160 Rab GTPase activating protein

Increased Phosphorylation of Akt Substrate of 160 kDa (AS160) in Rat Skeletal Muscle in Response to Insulin or Contractile Activity

Inhibition of GLUT4 Translocation by Tbc1d1, a Rab GTPase-activating Protein Abundant in Skeletal Muscle, Is Partially Relieved by AMP-activated Protein Kinase Activation

Insulin-Stimulated Phosphorylation of the Akt Substrate AS160 Is Impaired in Skeletal Muscle of Type 2 Diabetic Subjects

Temporal Dynamics of Tyrosine Phosphorylation in Insulin Signaling

κB-Ras Proteins Regulate Both NF-κB-Dependent Inflammation and Ral-Dependent Proliferation

Non-functional phosphorylations?

Insulin-stimulated Phosphorylation of the Rab GTPase-activating Protein TBC1D1 Regulates GLUT4 Translocation

A potential link between insulin signaling and GLUT4 translocation: Association of Rab10-GTP with the exocyst subunit Exoc6/6b

Mice lacking insulin receptor substrate 4 exhibit mild defects in growth, reproduction, and glucose homeostasis

Lipoatrophic diabetes in Irs1(-/-)/Irs3(-/-) double knockout mice

Calmodulin binds to the Rab GTPase activating protein required for insulin-stimulated GLUT4 translocation

Insulin stimulates the phosphorylation of the exocyst protein Sec8 in adipocytes

A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain

Insulin Receptor Substrate 4 Associates with the Protein IRAS

SPECHT — Single-stage phosphopeptide enrichment and stable-isotope chemical tagging: Quantitative phosphoproteomics of insulin action in muscle

Impact of Genetic Background and Ablation of Insulin Receptor Substrate (IRS)-3 on IRS-2 Knock-out Mice

The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the insulin receptor substrate family

Sequence and Structure of a Human Glucose Transporter

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