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Functional map of arrestin binding to phosphorylated opsin, with and without agonist.

  • Peterhans C Paul Scherrer Institute, Laboratory for Biomolecular Research, CH-5323, Villigen, Switzerland.
  • Lally CC Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117, Berlin, Germany.
  • Ostermaier MK Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117, Berlin, Germany.
  • Sommer ME Institut für Medizinische Physik und Biophysik (CC2), Charité-Universitätsmedizin Berlin, Charitéplatz 1, D-10117, Berlin, Germany.
  • Standfuss J Paul Scherrer Institute, Laboratory for Biomolecular Research, CH-5323, Villigen, Switzerland.
  • 2016-06-29
Published in:
  • Scientific reports. - 2016
Animals
Arrestin
Cattle
Models, Molecular
Mutation
Opsins
Protein Binding
Protein Domains
English Arrestins desensitize G protein-coupled receptors (GPCRs) and act as mediators of signalling. Here we investigated the interactions of arrestin-1 with two functionally distinct forms of the dim-light photoreceptor rhodopsin. Using unbiased scanning mutagenesis we probed the individual contribution of each arrestin residue to the interaction with the phosphorylated apo-receptor (Ops-P) and the agonist-bound form (Meta II-P). Disruption of the polar core or displacement of the C-tail strengthened binding to both receptor forms. In contrast, mutations of phosphate-binding residues (phosphosensors) suggest the phosphorylated receptor C-terminus binds arrestin differently for Meta II-P and Ops-P. Likewise, mutations within the inter-domain interface, variations in the receptor-binding loops and the C-edge of arrestin reveal different binding modes. In summary, our results indicate that arrestin-1 binding to Meta II-P and Ops-P is similarly dependent on arrestin activation, although the complexes formed with these two receptor forms are structurally distinct.
Language
  • English
Open access status
gold
Identifiers
Persistent URL
https://sonar.ch/global/documents/278332
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