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M306589200v1
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Papers In Press, published online ahead of print August 4, 2003
J. Biol. Chem, 10.1074/jbc.M306589200
Submitted on June 20, 2003
Revised on July 21, 2003
Accepted on August 4, 2003

Palmitoylation of the V2 vasopressin receptor carboxyl tail enhances beta arrestin recruitment leading to efficient receptor endocytosis and ERK1/2 activation

Pascale G. Charest and Michel Bouvier

Departement de Biochimie, Universite de Montreal, Montreal, Quebec H3C 3J7

Corresponding Author: michel.bouvier{at}umontreal.ca

A large number of G protein-coupled receptors are palmitoylated on cysteine residues located in their carboxyl tail but the general role of this post-translational modification remains poorly understood. Here we show that preventing palmitoylation of the V2 vasopressin receptor, by site directed mutagenesis of cysteines 341, 342, significantly delayed and decreased both agonist-promoted receptor endocytosis and mitogenactivated protein kinase activation. Pharmacological blockade of receptor endocytosis is without effect on the vasopressin-stimulated mitogenactivated protein kinase activity excluding the possibility that the reduced kinase activation mediated by the palmitoylation-less mutant could result from altered receptor endocytosis. In contrast, two dominant negative mutants of beta arrestin that inhibit receptor endocytosis also attenuated vasopressin-stimulated mitogen-activated protein kinase activity suggesting that the scaffolding protein, beta arrestin, represents the common link between receptor palmitoylation, endocytosis and kinase activation. Coimmunoprecipitation and bioluminescence resonance energy transfer experiments confirmed that inhibiting receptor palmitoylation considerably reduced the vasopressin-stimulated recruitment of beta arrestin to the receptor. Interestingly, the changes in beta arrestin recruitment kinetics were similar to those observed for vasopressin-stimulated receptor endocytosis and mitogenactivated protein kinase activation. Taken together the results indicate that palmitoylation enhances the recruitment of beta arrestin to the activated V2 vasopressin receptor thus facilitating processes requiring the scaffolding action of beta arrestin.


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