Monomeric rhodopsin is the minimal functional unit required for arrestin binding

Hisao Tsukamoto, Abhinav Sinha, Mark DeWitt, David L. Farrens

Research output: Contribution to journalArticlepeer-review

74 Scopus citations


We have tested whether arrestin binding requires the G-protein-coupled receptor be a dimer or a multimer. To do this, we encapsulated single-rhodopsin molecules into nanoscale phospholipid particles (so-called nanodiscs) and measured their ability to bind arrestin. Our data clearly show that both visual arrestin and β-arrestin 1 can bind to monomeric rhodopsin and stabilize the active metarhodopsin II form. Interestingly, we find that the monomeric rhodopsin in nanodiscs has a higher affinity for wild-type arrestin binding than does oligomeric rhodopsin in liposomes or nanodiscs, as assessed by stabilization of metarhodopsin II. Together, these results establish that rhodopsin self-association is not required to enable arrestin binding.

Original languageEnglish (US)
Pages (from-to)501-511
Number of pages11
JournalJournal of molecular biology
Issue number3
StatePublished - Jun 2010


  • Arrestin
  • G-protein-coupled receptor
  • Nanodiscs
  • Oligomerization
  • Rhodopsin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


Dive into the research topics of 'Monomeric rhodopsin is the minimal functional unit required for arrestin binding'. Together they form a unique fingerprint.

Cite this