Abstract
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 language | English (US) |
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Pages (from-to) | 501-511 |
Number of pages | 11 |
Journal | Journal of molecular biology |
Volume | 399 |
Issue number | 3 |
DOIs | |
State | Published - Jun 2010 |
Keywords
- Arrestin
- G-protein-coupled receptor
- Nanodiscs
- Oligomerization
- Rhodopsin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Molecular Biology