Monomeric rhodopsin is the minimal functional unit required for arrestin binding

J Mol Biol. 2010 Jun 11;399(3):501-11. doi: 10.1016/j.jmb.2010.04.029. Epub 2010 Apr 22.


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 beta-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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arrestin / chemistry*
  • Arrestins / chemistry*
  • Liposomes
  • Nanoparticles
  • Phospholipids
  • Phosphorylation
  • Protein Binding
  • Protein Multimerization
  • Rhodopsin / chemistry*
  • beta-Arrestins


  • Arrestin
  • Arrestins
  • Liposomes
  • Phospholipids
  • beta-Arrestins
  • metarhodopsins
  • Rhodopsin