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J. Biol. Chem., Vol. 281, Issue 23, 15780-15789, June 9, 2006

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Distinct Subcellular Localization for Constitutive and Agonist-modulated Palmitoylation of the Human Opioid Receptor^*

Ulla E. Petäjä-Repo¹, Mireille Hogue, Tarja T. Leskelä, Piia M. H. Markkanen, Jussi T. Tuusa, and Michel Bouvier²

From the Biocenter Oulu and Department of Anatomy and Cell Biology, University of Oulu, FI-90014, Oulu, Finland and Département de Biochimie, Université de Montréal, Montréal, Quebec 3C 3J7, Canada

Protein palmitoylation is a reversible lipid modification that plays important roles for many proteins involved in signal transduction, but relatively little is known about the regulation of this modification and the cellular location where it occurs. We demonstrate that the human opioid receptor is palmitoylated at two distinct cellular locations in human embryonic kidney 293 cells and undergoes dynamic regulation at one of these sites. Although palmitoylation could be readily observed for the mature receptor (M_r 55,000), [³H]palmitate incorporation into the receptor precursor (M_r 45,000) could be detected only following transport blockade with brefeldin A, nocodazole, and monensin, indicating that the modification occurs initially during or shortly after export from the endoplasmic reticulum. Blocking of palmitoylation with 2-bromopalmitate inhibited receptor cell surface expression, indicating that it is needed for efficient intracellular transport. However, cell surface biotinylation experiments showed that receptors can also be palmitoylated once they have reached the plasma membrane. At this location, palmitoylation is regulated in a receptor activation-dependent manner, as was indicated by the opioid agonist-promoted increase in the turnover of receptor-bound palmitate. This agonist-mediated effect did not require receptor-G protein coupling and occurred at the cell surface without the need for internalization or recycling. The activation-dependent modulation of receptor palmitoylation may thus contribute to the regulation of receptor function at the plasma membrane.

Received for publication, March 10, 2006

^* This work was supported by the Biocenter Oulu and Grant 200732 from the Academy of Finland (to U. E. P.-R.) and by the Canadian Institute for Health Research and the Heart and Stroke Foundation of Canada (to M. B.). 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 Research Fellow of the Academy of Finland. To whom correspondence may be addressed: Dept. of Anatomy and Cell Biology, University of Oulu, P. O. Box 5000, FI-90014, Oulu, Finland. Tel.: 358-8-537-5193; Fax: 358-8-537-5172; E-mail: Ulla.Petaja-Repo{at}oulu.fi. ² Holds the Canadian Research Chair in Signal Transduction and Molecular Pharmacology. To whom correspondence may be addressed: Dépt. de Biochimie, Faculté de Médicine, Université de Montréal, P. O. Box 6128, Succursale Centre-Ville, Montréal, Quebec H3C 3J7, Canada. Tel.: 514-343-6319; Fax: 514-343-2210; E-mail: Michel.Bouvier{at}umontreal.ca.

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