Ligand-independent GLUT4 translocation induced by guanosine 5'-O-(3-thiotriphosphate) involves tyrosine phosphorylation

Détails

ID Serval
serval:BIB_30B1623A2E88
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Ligand-independent GLUT4 translocation induced by guanosine 5'-O-(3-thiotriphosphate) involves tyrosine phosphorylation
Périodique
Endocrinology
Auteur(s)
Haruta  T., Morris  A. J., Vollenweider  P., Nelson  J. G., Rose  D. W., Mueckler  M., Olefsky  J. M.
ISSN
0013-7227 (Print)
Statut éditorial
Publié
Date de publication
01/1998
Volume
139
Numéro
1
Pages
358-64
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S. --- Old month value: Jan
Résumé
To delineate the signaling pathway leading to glucose transport protein (GLUT4) translocation, we examined the effect of microinjection of the nonhydrolyzable GTP analog, guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS), into 3T3-L1 adipocytes. Thirty minutes after the injection of 5 mM GTPgammaS, 40% of injected cells displayed surface GLUT4 staining indicative of GLUT4 translocation compared with 55% for insulin-treated cells and 10% in control IgG-injected cells. Treatment of the cells with the phosphatidylinositol 3-kinase inhibitor wortmannin or coinjection of GST-p85 SH2 fusion protein had no effect on GTPgammaS-mediated GLUT4 translocation. On the other hand, coinjection of antiphosphotyrosine antibodies (PY20) blocked GTPgammaS-induced GLUT4 translocation by 65%. Furthermore, microinjection of GTPgammaS led to the appearance of tyrosine-phosphorylated proteins around the periphery of the plasma membrane, as observed by immunostaining with PY20. Treatment of the cells with insulin caused a similar phosphotyrosine-staining pattern. Electroporation of GTPgammaS stimulated 2-deoxy-D-glucose transport to 70% of the extent of insulin stimulation. In addition, immunoblotting with phosphotyrosine antibodies after electroporation of GTPgammaS revealed increased tyrosine phosphorylation of several proteins, including 70- to 80-kDa and 120- to 130-kDa species. These results suggest that GTPgammaS acts upon a signaling pathway either downstream of or parallel to activation of phosphatidylinositol 3-kinase and that this pathway involves tyrosine-phosphorylated protein(s).
Mots-clé
1-Phosphatidylinositol 3-Kinase/physiology 3T3 Cells Adipocytes/metabolism Animals Biological Transport/drug effects Electroporation Glucose Transporter Type 4 Guanosine 5'-O-(3-Thiotriphosphate)/*pharmacology Mice Microinjections Molecular Weight Monosaccharide Transport Proteins/*metabolism *Muscle Proteins Phosphorylation Tyrosine/*metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/01/2008 14:06
Dernière modification de la notice
20/08/2019 13:15
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