Engineered hyperphosphorylation of the β2-adrenoceptor prolongs arrestin-3 binding and induces arrestin internalization.

ABSTRACT: G protein-coupled receptor phosphorylation plays a major role in receptor desensitization and arrestin binding. It is, however, unclear how distinct receptor phosphorylation patterns may influence arrestin binding and subsequent trafficking. Here we engineer phosphorylation sites into the C-terminal tail of the β2-adrenoceptor (β2AR) and demonstrate that this mutant, termed β2AR(SSS), showed increased isoprenaline-stimulated phosphorylation and differences in arrestin-3 affinity and trafficking. By measuring arrestin-3 recruitment and the stability of arrestin-3 receptor complexes in real time using fluorescence resonance energy transfer and fluorescence recovery after photobleaching, we demonstrate that arrestin-3 dissociated quickly and almost completely from the β2AR, whereas the intera

SUBMITTER: Zindel D 

PROVIDER: S-EPMC4293452 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature