GLUT8 subcellular localization and absence of translocation to the plasma membrane in PC12 cells and hippocampal neurons.

Détails

ID Serval
serval:BIB_EECF50BD048F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
GLUT8 subcellular localization and absence of translocation to the plasma membrane in PC12 cells and hippocampal neurons.
Périodique
Endocrinology
Auteur(s)
Widmer M., Uldry M., Thorens B.
ISSN
0013-7227
Statut éditorial
Publié
Date de publication
2005
Peer-reviewed
Oui
Volume
146
Numéro
11
Pages
4727-4736
Langue
anglais
Résumé
GLUT8 is a high-affinity glucose transporter present mostly in testes and a subset of brain neurons. At the cellular level, it is found in a poorly defined intracellular compartment in which it is retained by an N-terminal dileucine motif. Here we assessed GLUT8 colocalization with markers for different cellular compartments and searched for signals, which could trigger its cell surface expression. We showed that when expressed in PC12 cells, GLUT8 was located in a perinuclear compartment in which it showed partial colocalization with markers for the endoplasmic reticulum but not with markers for the trans-Golgi network, early endosomes, lysosomes, and synaptic-like vesicles. To evaluate its presence at the plasma membrane, we generated a recombinant adenovirus for the expression of GLUT8 containing an extracellular myc epitope. Cell surface expression was evaluated by immunofluorescence microscopy of transduced PC12 cells or primary hippocampal neurons exposed to different stimuli. Those included substances inducing depolarization, activation of protein kinase A and C, activation or inhibition of tyrosine kinase-linked signaling pathways, glucose deprivation, AMP-activated protein kinase stimulation, and osmotic shock. None of these stimuli-induced GLUT8 cell surface translocation. Furthermore, when GLUT8myc was cotransduced with a dominant-negative form of dynamin or GLUT8myc-expressing PC-12 cells or neurons were incubated with an anti-myc antibody, no evidence for constitutive recycling of the transporter through the cell surface could be obtained. Thus, in cells normally expressing it, GLUT8 was associated with a specific intracellular compartment in which it may play an as-yet-uncharacterized role.
Mots-clé
AMP-Activated Protein Kinases, Animals, Biological Transport, Cell Membrane, Electrophysiology, Enzyme Activation, Glucose, Glucose Transport Proteins, Facilitative, Hippocampus, Humans, Intracellular Membranes, Mice, Mice, Inbred C57BL, Microscopy, Fluorescence, Multienzyme Complexes, Neurons, Osmotic Pressure, PC12 Cells, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins c-myc, Rats, Recombinant Fusion Proteins, Signal Transduction, Subcellular Fractions, Tissue Distribution
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 14:41
Dernière modification de la notice
09/05/2019 3:10
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