The role of arrestins in the endocytosis and signalling of G protein-coupled receptors (GPCRs) is well established. Here, we report a new role for arrestin-3 in the anterograde transport of GPCRs. Overexpression of arrestin-3 promoted, while arrestin-3 knock-down by siRNA inhibited, the cell surface expression of the β2-adrenergic, the thromboxane A2 and the angiotensin II type 1 receptors in HEK293 cells. Surprisingly, we show that arrestin-3 binds directly to Gαs and Gαq, but not to Gαi proteins. An arrestin-3 mutant (arrestin-3 YRDR) deficient in Gαs and Gαq binding strongly inhibited the cell surface expression of the GPCRs that we studied. Confocal microscopy revealed that arrestin-3 can localize at the Golgi where the arrestin-3 YRDR mutant retained the receptors. We also report that arrestin-3 interact with the COPI complex of proteins involved in Golgi vesicular transport. Interestingly, we observed that Gα proteins were co-immunoprecipitated with COPI, which was promoted by overexpression of arrestin-3. We propose a new model where arrestin-3 regulates the anterograde transport of GPCRs by forming a molecular complex with Gα proteins and COPI.