The type 1 angiotensin (AT1) receptor mediates the homeostatic and pathological actions of the peptide hormone, angiotensin II. With regard to the processes that activate and deactivate seven-transmembranespanning, G-protein-coupled receptors (GPCRs), AT1 receptors are among the most widely studied, serving as prototypes for GPCRs that bind and respond to peptide hormones. Arrestins are proteins that bind to activated and phosphorylated GPCRs, terminating initial signals emanating from these receptors, in addition to mediating receptor internalization. New aspects of arrestin function continue to emerge, such as their capacity to act as scaffolds to recruit regulatory and signaling molecules to increase the repertoire of receptor responses. Here, we examine the evidence that arrestins contribute to the signaling, deactivation and trafficking of AT1 receptors.