Monomeric Rhodopsin Is the Minimal Functional Unit Required for Arrestin Binding |
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Authors: | Hisao Tsukamoto Abhinav Sinha David L Farrens |
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Institution: | 1 Department of Biochemistry and Molecular Biology, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Portland, OR 97239-3098, USA 2 Department of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan |
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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. |
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Keywords: | GPCR G-protein-coupled receptor ROS rod outer segments MSP membrane scaffold protein apo A-1 apolipoprotein A-1 meta-II metarhodopsin II WT wild type POPC 1-palmitoyl-2-oleoyl phosphatidylcholine POPG 1-palmitoyl-2-oleoyl phosphatidylglycerol meta-I metarhodopsin I FRET fluorescence energy transfer ConA concanavalin A |
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