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Originally published In Press as doi:10.1074/jbc.M108398200 on November 29, 2001

J. Biol. Chem., Vol. 277, Issue 8, 5891-5901, February 22, 2002
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Constitutive Internalization of Constitutively Active Angiotensin II AT1A Receptor Mutants Is Blocked by Inverse Agonists*

Stéphanie Miserey-LenkeiDagger , Charles ParnotDagger , Sabine BardinDagger , Pierre Corvol§, and Eric ClauserDagger

From Dagger  INSERM EPI 0103, Institut Cochin, 24 rue du Faubourg Saint-Jacques, 75014 Paris, France and § INSERM U36, Collège de France, 11 place Marcelin Berthelot, 75005 Paris, France

As constitutively active mutants (CAMs) mimic an active conformation, they can be used to characterize the process of G protein-coupled receptor activation. Here, we used CAMs to study the link between activation and internalization of the angiotensin II AT1A receptor. The cellular localization of fluorescently tagged N111A, I245T, and L305Q mutants was determined by confocal microscopy. In the absence of ligand, CAMs were mostly located in intracellular vesicles, whereas the wild-type AT1A was found at the cell surface. After 2 h incubation with inverse agonist, losartan, CAMs were translocated to the plasma membrane. Similar observations were made in H295, a human adrenocortical cell line which expresses physiologically the AT1 receptor. This phenomenon, which was not dependent on protein synthesis and the pharmacology and kinetics of which were similar to the recycling of the wild-type receptor, was called "externalization". After externalization and losartan removal, the L305Q CAM underwent rapid ligand-independent endocytocis, with the same kinetics and temperature sensitivity as the angiotensin II-induced internalization of the wild-type AT1A. Moreover, the addition of a second mutation known to block internalization (Delta 329 truncation) prevented intracellular localization of the CAM. These data show that AT1A CAMs are constitutively and permanently internalized and recycled. This mechanism is different from the down-regulation observed for CAMs of other G protein-coupled receptors and thus defines a new paradigm for the cellular regulation of CAMs.

* This work was supported by Grant 98126 from Hoescht Marion Roussel and the Institut National Pour la Santé and la Recherche Médicale (INSERM).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: INSERM EPI 0103-ICGM, Faculté de Médecine Cochin, Port Royal, 24 rue du Fg St Jacques, 75014 Paris, France. Tel.: 33-1-53-73-27-50; Fax: 33-1-53-73-27-51; E-mail: clauser@cochin.inserm.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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