Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 399, Issue 3, Pages 501-511Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.04.029
Keywords
rhodopsin; G-protein-coupled receptor; arrestin; oligomerization; nanodiscs
Categories
Funding
- National Institutes of Health [DA018169, EY015436]
- Japan Society for the Promotion of Science for Young Scientists
- Uehara Memorial Foundation
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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. (C) 2010 Elsevier Ltd. All rights reserved.
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