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J. Biol. Chem., Vol. 277, Issue 38, 34666-34673, September 20, 2002
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From the Department of Cell Biology, Cochin Institute, INSERM
U-567, CNRS UMR-8104 and University René-Descartes, Paris 75014, France, the § Department of Biochemistry, University of
Montreal, Montreal, Quebec H3C 3J7, Canada, and the
¶ Institut de Recherche Interdisciplinaire en Biologie Humaine et
Nucléaire, Université Libre de Bruxelles, B-1070
Bruxelles, Belgium
Although homo-oligomerization has been
reported for several G protein-coupled receptors, this phenomenon was
not studied at low concentrations of receptors. Furthermore, it is not
clear whether homo-oligomerization corresponds to an intrinsic property of nascent receptors or if it is a consequence of receptor activation. Here CCR5 receptor oligomerization was studied by bioluminescence resonance energy transfer (BRET) in cells expressing physiological levels of receptors. A strong energy transfer could be observed, in the
absence of ligands, in whole cells and in both endoplasmic reticulum and plasma membrane subfractions, supporting the hypothesis of a constitutive oligomerization that occurs early after biosynthesis. No change in BRET was observed upon agonist binding, indicating that
the extent of oligomerization is unrelated to the activation state of
the receptor. In contrast, a robust increase of BRET, induced by a
monoclonal antibody known to promote receptor clustering, suggests that
microaggregation of preformed receptor homo-oligomers can occur. Taken
together, our data indicate that constitutive receptor
homo-oligomerization has a biologically relevant significance and might
be involved in the process of receptor biosynthesis.
Constitutive Agonist-independent CCR5 Oligomerization and
Antibody-mediated Clustering Occurring at Physiological Levels of
Receptors*,
,
, and
*
This work was supported by grants from the Agence
Nationale pour la Recherche sur le SIDA the Association pour la
Recherche sur le Cancer, the Actions de Recherche Concertées of
the Communauté Française de Belgique, and the Canadian
Institute for Health Research.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.
The on-line version of this article (available at
http://www.jbc.org) contains additional text and one figure.
Recipient of a fellowship from the Association pour la Recherche
sur la Polyarthrite Rhumatoïde.
Holder of a Canada Research Chair in Molecular and Cellular Pharmacology.
**
To whom correspondence should be addressed: Dépt.
de Biologie Cellulaire, Institut Cochin, Bât. G Roussy, 27, rue
du Fg. St. Jacques 75014 Paris, France. Tel.: 331-44-41-25-58; Fax:
331-44-41-25-57; E-mail: marullo@cochin.inserm.fr.
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