Molecular mechanism of phosphorylation-dependent arrestin activation

- Novel structures provide insight into the arrestin activation mechanism.
- Arrestins are pre-activated by a C-tail exchange mechanism.
- Functional data for arrestin-1 are largely transferable to other arrestin subtypes.
- Three clusters of conserved phosphate sensors establish high affinity interactions.
- Arrestins provide tunable phosphate sensors for differentially phosphorylated GPCRs.