Historically, dopamine receptors (DARs) and other G protein-coupled receptors (GPCRs) were believed to be independent signaling units in the plasma membrane, interacting only transiently with G proteins to initiate a downstream signaling cascade. However, in recent years it has become clear that DARs do not function in isolation, but in fact exist as members of macromolecular protein complexes. The DAR protein complex, or the signalplex, consists of a variety of protein interactors that may be transient or stable in nature and that are collectively referred to as dopamine receptor-interacting proteins (DRIPs). Ultimately, the goal of the signalplex is to organize the cellular machinery or signaling components that are critical to the DAR at any given time in an orderly fashion. This higher level of organization around the DAR enables the receptor to process all information, from extracellular ligands or intracellular signaling molecules, and propagate the necessary cellular response in a timely and efficient manner.