Analysis of temporal patterns of GPCR–β-arrestin interactions using split luciferase-fragment complementation

Abstract

We developed bioluminescence probes to detect quantitative interaction of GPCRs with arrestin isoforms β-arrestin1 and β-arrestin2 based on split luciferase complementation. Time-dependent GPCR–β-arrestin interactions showed two-types of remarkable variations that were consistent with a classification of GPCR classes. Positive charge residues in serine clusters located at the C-terminal region of GPCRs were necessary for binding to β-arrestin. This quantitative method enables elucidation of the mechanisms of different classes of GPCRs that regulate β-arrestin isoforms.