Protein Kinase B Stimulates the Translocation of GLUT4 but Not GLUT1 or Transferrin Receptors in 3T3-L1 Adipocytes by a Pathway Involving SNAP-23, Synaptobrevin-2, and/or Cellubrevin
| Autor: | LM Fletcher, Paru B. Oatey, J. Oliver Dolly, Patrick G. Foran, Jeremy M. Tavaré, Nadiem Mohammed |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Botulinum Toxins
Monosaccharide Transport Proteins Vesicle-Associated Membrane Protein 3 Endosome Green Fluorescent Proteins Muscle Proteins Chromosomal translocation Transferrin receptor Clostridium difficile toxin B Protein Serine-Threonine Kinases Biology Biochemistry R-SNARE Proteins Mice Proto-Oncogene Proteins Receptors Transferrin Adipocytes Animals Humans Insulin Amino Acid Sequence Qc-SNARE Proteins Receptor Molecular Biology Protein kinase B Glucose Transporter Type 1 Glucose Transporter Type 4 Hydrolysis Glucose transporter Membrane Proteins nutritional and metabolic diseases Biological Transport 3T3 Cells Cell Biology Qb-SNARE Proteins Molecular biology Cell biology Luminescent Proteins Zinc biology.protein Carrier Proteins Proto-Oncogene Proteins c-akt hormones hormone substitutes and hormone antagonists GLUT4 |
| Zdroj: | Journal of Biological Chemistry. 274:28087-28095 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.274.40.28087 |
| Popis: | An interaction of SNAP-23 and syntaxin 4 on the plasma membrane with vesicle-associated synaptobrevin-2 and/or cellubrevin, known as SNAP (soluble N -ethyl-maleimide-sensitive factorattachment protein) receptors or SNAREs, has been proposed to provide the targeting and/or fusion apparatus for insulin-stimulated translocation of the GLUT4 isoform of glucose transporter to the plasma membrane. By microinjecting 3T3-L1 adipocytes with the Clostridium botulinum toxin B or E, which proteolyzed synaptobrevin-2/cellubrevin and SNAP-23, respectively, we investigated the role of these SNAREs in GLUT4, GLUT1, and transferrin receptor trafficking. As expected, insulin stimulated the translocation of GLUT4, GLUT1, and transferrin receptors to the plasma membrane. By contrast, a constitutively active protein kinase B (PKB-DD) only stimulated a translocation of GLUT4 and not GLUT1 or the transferrin receptor. The GLUT4 response to PKB-DD was abolished by toxins B or E, whereas the insulin-evoked translocation of GLUT4 was inhibited by approximately 65%. These toxins had no significant effect on insulin-stimulated transferrin receptor appearance at the cell surface. Thus, insulin appears to induce GLUT4 translocation via two distinct routes, only one of which involves SNAP-23 and synaptobrevin-2/cellubrevin, and can be mobilized by PKB-DD. The PKB-, SNAP-23-, and synaptobrevin-2/cellubrevin-independent GLUT4 translocation pathway may involve movement through recycling endosomes, together with GLUT1 and transferrin receptors. |
| Databáze: | OpenAIRE |
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