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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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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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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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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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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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Insulin Receptor Substrate 3 Is Not Essential for Growth or Glucose Homeostasis

The Journal of biological chemistry, 1999-06, Vol.274 (25), p.18093-18099

1999

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Synip phosphorylation does not regulate insulin-stimulated GLUT4 translocation

Biochemical and biophysical research communications, 2005-07, Vol.332 (3), p.880-884

2005

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Increased intracellular sequestration of the insulin-regulated aminopeptidase upon differentiation of 3T3-L1 cells

Biochemical journal, 1998-03, Vol.330 ( Pt 2) (2), p.1003-1008

1998

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Adipocytes contain a novel complex similar to the tuberous sclerosis complex

Cellular signalling, 2006-10, Vol.18 (10), p.1626-1632

2006

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Novel insulin-elicited phosphoproteins in adipocytes

Cellular signalling, 2005, Vol.17 (1), p.59-66

2005

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Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes

The Journal of biological chemistry, 1998-02, Vol.273 (6), p.3582-3587

1998

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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

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

Temporal Dynamics of Tyrosine Phosphorylation in Insulin Signaling

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

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

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

Insulin Receptor Substrate 3 Is Not Essential for Growth or Glucose Homeostasis

Synip phosphorylation does not regulate insulin-stimulated GLUT4 translocation

Increased intracellular sequestration of the insulin-regulated aminopeptidase upon differentiation of 3T3-L1 cells

Adipocytes contain a novel complex similar to the tuberous sclerosis complex

Novel insulin-elicited phosphoproteins in adipocytes

Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes

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