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The dopamine D 1  receptor (D 1 R), a G protein-coupled receptor, plays a critical role in regulating blood pressure through its actions on renal hemodynamics and epithelial ion transport, which are highly linked to its intracellular trafficking. In this study, we generated a series of C-terminal mutants of D 1 R that were tagged with or without enhanced yellow fluorescent protein, and analyzed the consequences of these mutants on the plasma membrane trafficking of D 1 R and cyclic AMP response to D 1 R stimulation. D 1 R with mutations within the endocytic recycling signal (amino acid residues 360–382) continued to be functional, albeit decreased relative to wild-type D 1 R. Mutation of the palmitoylation site (347C>S) of D 1 R did not impair its trafficking to the plasma membrane, but abolished its ability to increase cyclic AMP accumulation. In contrast, replacement of di-leucines (344–345L>A) by alanines resulted in the retention of D 1 R in the early endosome, decreased its glycosylation, and prevented its targeting to the plasma membrane. Our studies suggest that di-L motif at the C-terminus of D 1 R is critical for the glycosylation and cell surface targeting of D 1 R.

C-Terminal Di-leucine Motif of Dopamine D1 Receptor Plays an Important Role in Its Plasma Membrane Trafficking