摘要
We developed bioluminescence probes to detect quantitative interaction of GPCRs with arrestin isoforms beta-arrestin1 and beta-arrestin2 based on split luciferase complementation. Time-dependent GPCR-beta-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 beta-arrestin. This quantitative method enables elucidation of the mechanisms of different classes of GPCRs that regulate beta-arrestin isoforms.
- 出版日期2013