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The Rhodopsin-Arrestin-1 Interaction in Bicelles

Chen, Qiuyan, Vishnivetskiy, Sergey A., Zhuang, Tiandi, Cho, Min-Kyu, Thaker, Tarjani M., Sanders, Charles R., Gurevich, Vsevolod V. and Iverson, T. M. (2015) The Rhodopsin-Arrestin-1 Interaction in Bicelles. Methods in molecular biology, 1271. pp. 77-95. ISSN 1940-6029; 1064-3745


G-protein-coupled receptors (GPCRs) are essential mediators of information transfer in eukaryotic cells. Interactions between GPCRs and their binding partners modulate the signaling process. For example, the interaction between GPCR and cognate G protein initiates the signal, while the interaction with cognate arrestin terminates G-protein-mediated signaling. In visual signal transduction, arrestin-1 selectively binds to the phosphorylated light-activated GPCR rhodopsin to terminate rhodopsin signaling. Under physiological conditions, the rhodopsin-arrestin-1 interaction occurs in highly specialized disk membrane in which rhodopsin resides. This membrane is replaced with mimetics when working with purified proteins. While detergents are commonly used as membrane mimetics, most detergents denature arrestin-1, preventing biochemical studies of this interaction. In contrast, bicelles provide a suitable alternative medium. An advantage of bicelles is that they contain lipids, which have been shown to be necessary for normal rhodopsin-arrestin-1 interaction. Here we describe how to reconstitute rhodopsin into bicelles, and how bicelle properties affect the rhodopsin-arrestin-1 interaction.

Item Type: Article
Date Deposited: 21 Mar 2019 00:45
Last Modified: 21 Mar 2019 00:45


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