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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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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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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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truncation mutation in TBC1D4 in a family with acanthosis nigricans and postprandial hyperinsulinemia

Proceedings of the National Academy of Sciences - PNAS, 2009-06, Vol.106 (23), p.9350-9355

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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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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Stoichiometry of Site-Specific Protein Phosphorylation Estimated with Phosphopeptide-Specific Antibodies

BioTechniques, 2003-04, Vol.34 (4), p.828-831

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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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

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

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?

truncation mutation in TBC1D4 in a family with acanthosis nigricans and postprandial hyperinsulinemia

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

Sequence and Structure of a Human Glucose Transporter

Stoichiometry of Site-Specific Protein Phosphorylation Estimated with Phosphopeptide-Specific Antibodies

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

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