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Originally published In Press as doi:10.1074/jbc.M205663200 on January 15, 2003

J. Biol. Chem., Vol. 278, Issue 14, 12222-12230, April 4, 2003
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The Metabotropic Glutamate Receptor mGluR5 Is Endocytosed by a Clathrin-independent Pathway*

Lawrence FourgeaudDagger , Anne-Sophie Bessis§, Françoise RossignolDagger , Jean-Philippe Pin§, Jean-Christophe Olivo-Marin, and Agnès HémarDagger ||

From the Dagger  "Physiologie Cellulaire de la Synapse," UMR 5091 CNRS/Université Bordeaux 2, Institut François Magendie, Rue Camille Saint Saëns, 33077 Bordeaux Cedex, France, § "Mécanismes Moléculaires des Communications Cellulaires," UPR CNRS 9023, CCIPE, 141 Rue de la Cardonille, 34094 Montpellier Cedex 5, France, and  "Analyse d'Images Quantitative," URA CNRS 1947, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris Cedex, France

Metabotropic glutamate receptors 5 (mGluR5) are members of the growing group C G protein-coupled receptor family. Widely expressed in mammalian brain, they are involved in modulation of the glutamate transmission. By means of transfection of mGluR5 receptors in COS-7 cells and primary hippocampal neurons in culture followed by immunocytochemistry and quantitative image analysis and by a biochemical assay, we have studied the internalization of mGluR5 splice variants. mGluR5a and -5b were endocytosed in COS-7 cells as well as in axons and dendrites of cultured neurons. Endocytosis occurred even in the absence of receptor activity, because receptors mutated in the glutamate binding site were still internalized as well as receptors in which endogenous activity had been inhibited by an inverse agonist. We have measured a constitutive rate of endocytosis of 11.7%/min for mGluR5a. We report for the first time the endocytosis pathway of mGluR5. Internalization of mGluR5 is not mediated by clathrin-coated pits. Indeed, inhibition of this pathway by Eps15 dominant negative mutants did not disturb their endocytosis. However, the large GTPase dynamin 2 is implicated in the endocytosis of mGluR5 in COS-7. mGluR5 is the first shown member of the group C G-protein coupled receptor family internalized by a nonconventional pathway.

* This work was supported by grants from the Conseil Régional d'Aquitaine, the Association pour la Recherche Médicale en Aquitaine.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed. Tel.: 33-5-57-57-40-89; Fax: 33-5-57-57-40-82; E-mail: ahemar@u-bordeaux2.fr.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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