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Papers In Press, published online ahead of print July 14, 2003
Pharmacology Dept., University of Minnesota, Minneapolis, MN 55455
Corresponding Author: qiuxx014{at}umn.edu
It is generally accepted that the internalization and desensitization of
J. Biol. Chem, 10.1074/jbc.M305857200
Submitted on June 4, 2003
Revised on July 11, 2003
Accepted on July 14, 2003
-opioid receptor desensitization: role of receptor phosphorylation, internalization and resensitization
-opioid receptor (MOR) involves receptor phosphorylation and 
-arrestin recruitment. However, a mutant MOR, which is truncated after the amino acid residue Ser363 (MOR363D), was found to undergo phosphorylation-independent internalization and desensitization. As expected, MOR363D, missing the putative agonist-induced phosphorylation sites, did not exhibit detectable agonist-induced phosphorylation. MOR363D underwent slower internalization as reflected in the attenuation of membrane translocation of -arrestin 2 when compared with wild type MOR, but the level of receptor being internalized was similar to that of wild type MOR after 4 h of etorphine treatment. Furthermore, MOR363D was observed to desensitize faster than that of wild type MOR upon agonist activation. Surface biotinylation assay demonstrated that the wild type receptors recycled back to membrane after agonist-induced internalization, which contributed to the receptor resensitization and thus partially reversed the receptor desensitization. On the contrary, MOR363D did not recycle after internalization. Hence, MOR desensitization is controlled by the receptor internalization and the recycling of internalized receptor to cell surface in an active state. Taken together, our data indicated that receptor phosphorylation is not absolutely required in the internalization but receptor phosphorylation and subsequent -arrestin recruitment play important roles in the resensitization of internalized receptors.
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