The basic module of signal transduction that involves G-protein-coupled receptors is usually portrayed as comprising a receptor, a heterotrimeric G protein and an effector. It is now well established that regulated interactions between receptors and arrestins, and between G proteins and regulators of G-protein signalling alter the effectiveness and kinetics of information transfer. However, more recent studies have begun to identify a host of other proteins that interact selectively with individual receptors at both the intracellular and extracellular face of the membrane. Although the functional relevance of many of these interactions is only beginning to be understood, current information indicates that these interactions might determine receptor properties, such as cellular compartmentalization or signal selection, and can promote protein scaffolding into complexes that integrate function.