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J. Biol. Chem., Vol. 280, Issue 43, 36195-36205, October 28, 2005

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The Intracellular Trafficking of the G Protein-coupled Receptor TP Depends on a Direct Interaction with Rab11^*

From the Service de Rhumatologie, FacultédeMédecine and Centre de Recherche Clinique-CHUS, Université de Sherbrooke, Sherbrooke, Québec J1H 5N4, Canada

Intracellular trafficking pathways of cell surface receptors following their internalization are the subject of intense research efforts. However, the mechanisms by which they recycle back to the cell surface are still poorly defined. We have recently demonstrated that the small Rab11 GTPase protein is a determinant factor in controlling the recycling to the cell surface of the -isoform of the thromboxane A₂ receptor (TP) following its internalization. Here, we demonstrate with co-immunoprecipitation studies in HEK293 cells that there is a Rab11-TP association occurring in the absence of agonist, which is not modulated by stimulation of TP. We show with purified TP intracellular domains fused to GST and HIS-Rab11 proteins that Rab11 interacts directly with the first intracellular loop and the C-tail of TP. Amino acids 335–344 of the TP C-tail were determined to be essential for the interaction of Rab11 with this receptor domain. This identified sequence appears to be important in directing the intracellular trafficking of the receptor from the Rab5-positive intracellular compartment to the perinuclear recycling endosome. Interestingly, our data indicate that TP interacts with the GDP-bound form, and not the GTP-bound form, of Rab11 which is necessary for recycling of the receptor back to the cell surface. To our knowledge, this is the first demonstration of a direct interaction between Rab11 and a transmembrane receptor.

Received for publication, March 29, 2005 , and in revised form, August 24, 2005.

^* This work was supported by a grant (to J.-L. P.) from the Canadian Institutes of Health Research (CIHR). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by a fellowship from the Fonds de la Recherche en Santé du Québec.

² Recipient of a CIHR New Investigator Award. To whom correspondence should be addressed: Service de Rhumatologie, FacultédeMédecine, Université de Sherbrooke, 3001 12^e Ave. Nord, Fleurimont, QC J1H 5N4, Canada. Tel.: 819-564-5264; Fax: 819-564-5265; E-mail: jean-luc.parent{at}USherbrooke.ca.

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