Single-molecule analysis of GPCR-mediated β-arrestin activation

Abstract

β-arrestins bind G protein-coupled receptors (GPCRs) to terminate G-protein signaling and to facilitate other downstream signaling pathways. During activation, β-arrestin's carboxy-terminal tail must disengage from the amino-terminal domain, but little is known about this process. Here, we use single-molecule fluorescence resonance energy transfer imaging of β-arrestin1, alone and in complex with activating phosphorylated receptor carboxy-terminal tail mimetics or full-length receptor, to explore β-arrestin tail dynamics.