Phosphorylation and Palmitoylation of the Human D2<sub><nobr>L</nobr></sub> Dopamine Receptor in Sf9 Cells期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Phosphorylation and Palmitoylation of the Human D2_L Dopamine Receptor in Sf9 Cells

Authors:	Gordon Y K Ng †Brian F O'Dowd ‡Mirelle Caron ‡Michael Dennis §Mark R Brann † Susan R George

Institution:	Addiction Research Foundation, and; Department of Pharmacology, University of Toronto, Toronto, Ontario, and; Biosignal Inc., Montreal, Quebec, Canada;and; Molecular Neuropharmacology Section, Department of Psychiatry, and Vermont Comprehensive Cancer Center, University of Vermont, Burlington, Vermont, U.S.A.

Abstract:	Abstract: We have expressed and biochemically characterized the human D2_long (D2_L) dopamine receptor isoform using the baculovirus/Sf9 cell system. The expressed receptor bound ligands with a pharmacological profile similar to that reported for neuronal and cloned D2_L receptors expressed in mammalian cell lines. Dopamine binding to D2_L receptor was sensitive to guanine nucleotides, indicating receptor coupling to endogenous G proteins. A D2_L receptor-specific antibody identified two major protein species at ～44 kDa and at ～93 kDa in immunoblots, suggesting the presence of D2_L receptor monomers and dimers. Both species were purified by immunoprecipitation from digitonin-solubilized preparation of cells expressing D2_L receptor prelabeled with ³²P_i or ³H]-palmitate. These results constitute the first direct evidence for D2_L receptor phosphorylation and palmitoylation.

Keywords:	Baculovirus/Sf9 Phosphorylation Palmitoylation D2 receptor antibody

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