Investigators studied β-arrestins (βarrs), crucial proteins in seven transmembrane receptor (7TMR) signaling. Using cryo–electron microscopy, they captured seven structural states of βarrs, showcasing their interactions in basal, muscarinic receptor subtype 2 (M2R)-activated, and βarr-biased decoy D6 receptor (D6R)-activated states. These snapshots unveil unique βarr-7TMR engagements and reveal a structural shift in βarr2’s carboxyl terminus upon D6R activation. The findings provide unexpected molecular insights into 7TMR-βarr complexes, offering potential therapeutic avenues.