Insulin controls the spatial distribution of GLUT4 on the cell surface through regulation of its postfusion dispersal. - sprookjes - yvandenbroek - TriplyDB

Insulin controls the spatial distribution of GLUT4 on the cell surface through regulation of its postfusion dispersal.

Insulin controls the spatial distribution of GLUT4 on the cell surface through regulation of its postfusion dispersal.

http://www.wikidata.org/entity/Q36189207

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Insulin regulates Glut4 confinement in plasma membrane clusters in adipose cells Biomolecular Characterization of Putative Antidiabetic Herbal Extracts Insulin stimulates syntaxin4 SNARE complex assembly via a novel regulatory mechanism Kv2.1 cell surface clusters are insertion platforms for ion channel delivery to the plasma membrane AS160 phosphotyrosine-binding domain constructs inhibit insulin-stimulated GLUT4 vesicle fusion with the plasma membrane Translocation of mixed lineage kinase domain-like protein to plasma membrane leads to necrotic cell death Resin embedded multicycle imaging (REMI): a tool to evaluate protein domains.Insulin stimulates fusion, but not tethering, of GLUT4 vesicles in skeletal muscle of HA-GLUT4-GFP transgenic mice Imaging the post-fusion release and capture of a vesicle membrane protein Plasma membrane domains enriched in cortical endoplasmic reticulum function as membrane protein trafficking hubs Novel effects of Brefeldin A (BFA) in signaling through the insulin receptor (IR) pathway and regulating FoxO1-mediated transcription.Spatiotemporal Regulators for Insulin-Stimulated GLUT4 Vesicle Exocytosis.Role of clusters in insulin-regulated GLUT4 trafficking in adipose cells: a new paradigm?Munc18c: a controversial regulator of peripheral insulin action.Signaling, cytoskeletal and membrane mechanisms regulating GLUT4 exocytosis.Kinetic evidence that Glut4 follows different endocytic pathways than the receptors for transferrin and alpha2-macroglobulin.Human adipose cells in vitro are either refractory or responsive to insulin, reflecting host metabolic state Dual-mode of insulin action controls GLUT4 vesicle exocytosis.GLUT4 exocytosis.Dual Effect of Rosuvastatin on Glucose Homeostasis Through Improved Insulin Sensitivity and Reduced Insulin Secretion.Statistical Frailty Modeling for Quantitative Analysis of Exocytotic Events Recorded by Live Cell Imaging: Rapid Release of Insulin-Containing Granules Is Impaired in Human Diabetic β-cells Rosiglitazone drives cavin-2/SDPR expression in adipocytes in a CEBPα-dependent manner.Cardiac PI3K-Akt impairs insulin-stimulated glucose uptake independent of mTORC1 and GLUT4 translocation.Direct chemical evidence for sphingolipid domains in the plasma membranes of fibroblasts Optogenetic activation reveals distinct roles of PIP3 and Akt in adipocyte insulin action.Impaired tethering and fusion of GLUT4 vesicles in insulin-resistant human adipose cells.Trapping by clusters of channels, receptors, and transporters: quantitative description.SNARE proteins underpin insulin-regulated GLUT4 traffic.Making a big thing of a small cell--recent advances in single cell analysis.Studies of the regulated assembly of SNARE complexes in adipocytes.A systems biology analysis connects insulin receptor signaling with glucose transporter translocation in rat adipocytes.Glut4 palmitoylation at Cys223 plays a critical role in Glut4 membrane trafficking Alternative routes to the cell surface underpin insulin-regulated membrane trafficking of GLUT4.Visualization and quantitation of GLUT4 translocation in human skeletal muscle following glucose ingestion and exercise.Grp1 plays a key role in linking insulin signaling to glut4 recycling PKA-independent cAMP stimulation of white adipocyte exocytosis and adipokine secretion: modulations by Ca2+ and ATP.DHHC7 Palmitoylates Glucose Transporter 4 (Glut4) and Regulates Glut4 Membrane Translocation.Novel systems for dynamically assessing insulin action in live cells reveals heterogeneity in the insulin response.Identification of Insulin-Activated Rab Proteins in Adipose Cells Using Bio-ATB-GTP Photolabeling Technique.Glucose Transport: Methods for Interrogating GLUT4 Trafficking in Adipocytes.

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P2860

Insulin controls the spatial distribution of GLUT4 on the cell surface through regulation of its postfusion dispersal.

http://www.wikidata.org/entity/Q36189207

description

2010 nî lūn-bûn

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年學術文章

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2010年學術文章

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2010年學術文章

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name

Insulin controls the spatial d ...... n of its postfusion dispersal.

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Insulin controls the spatial d ...... n of its postfusion dispersal.

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Insulin controls the spatial d ...... n of its postfusion dispersal.

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Insulin controls the spatial d ...... n of its postfusion dispersal.

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Insulin controls the spatial d ...... n of its postfusion dispersal.

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Insulin controls the spatial d ...... n of its postfusion dispersal.

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J.CMET.2010.08.005

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Cell Metabolism

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Insulin controls the spatial d ...... n of its postfusion dispersal.

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Joshua Zimmerberg

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Karin G Stenkula

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Samuel W Cushman

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Vladimir A Lizunov

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P2860

Functional cloning of TUG as a regulator of GLUT4 glucose transporter trafficking

Sortilin is essential and sufficient for the formation of Glut4 storage vesicles in 3T3-L1 adipocytes

Clathrin-dependent and independent endocytosis of glucose transporter 4 (GLUT4) in myoblasts: regulation by mitochondrial uncoupling

Insulin signaling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane

Insulin stimulates membrane fusion and GLUT4 accumulation in clathrin coats on adipocyte plasma membranes.

Direct quantification of fusion rate reveals a distal role for AS160 in insulin-stimulated fusion of GLUT4 storage vesicles.

Insulin regulates fusion of GLUT4 vesicles independent of Exo70-mediated tethering.

Characterization of a distinct plasma membrane macrodomain in differentiated adipocytes.

Dynamic tracking and mobility analysis of single GLUT4 storage vesicle in live 3T3-L1 cells.

Lipid rafts are required for GLUT4 internalization in adipose cells.

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250-259

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10.1016/J.CMET.2010.08.005

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3

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12

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20816091

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