Dopaminergic signaling in the central nervous system is regulated by the human dopamine (DA) transporter (hDAT) molecules. DAT maintains the synaptic concentration of DA at physiological levels, upon reuptake of DA into presynaptic terminals thus preventing the saturation or desensitization of dopamine receptors.  DA translocation involves the co-transport of two sodium ions and the channeling of a chloride ion, and it is achieved via alternating access between outward-facing and inward-facing states of DAT. hDAT is a target for addictive drugs, such as cocaine, amphetamine (AMPH), and therapeutic antidepressants. However, the molecular mechanism of dopamine transport and its modulation by psychostimulants remain elusive. The newly resolved DAT structure from Drosophila melanogaster recently opened the way to a deeper understanding of the mechanism and time evolution of DAT function. Simulations also demonstrated that binding DA or AMPH drives a structural transition toward a functional form predisposed to translocate the ligand.  I will present recent progress in this topic obtained with a combination of computational models and methods that now provide deeper insights into the complex mechanism of hDAT function, and the role of intermolecular interactions in the regulation of dopaminergic signaling.