※ Arrestin family introduction

    Arrestins comprise a family of four known members in mammals: two visual arrestins, 1 and 4, found in the rod and cone cells of the retina, and two nonvisual arrestins, 2 and 3, which are found in most other tissues of the body. The current model of arrestin-mediated interactions with ligand-occupied GPCRs holds that, after ligand occupancy, cytoplasmic regions of the receptor are phosphorylated at serine and threonine residues by a member of the family of G protein-coupled receptor kinases. Upon arrestin binding, these phosphorylated residues disrupt arrestin's polar core, inducing a conformational change within the molecule that allows it to interact further with the receptor. Recent study examined the interactions between members of the arrestin family with the phosphorylated carboxyl-terminal domain of the FPR using a bead-based, cell-free assay (1).

Reference
1. Potter, R.M. (2002) Arrestin variants display differential binding characteristics for the phosphorylated N-formyl peptide receptor carboxyl terminus . Curr Protein Pept Sci, 12, 3-11. PMID: 11777932