C-edge loops of arrestin function as a membrane anchor

Ciara C M. Lally, Brian Bauer, Jana Selent () and Martha E Sommer ()
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Ciara C M. Lally: Institute of Medical Physics and Biophysics (CC2), Charité Medical University
Brian Bauer: Institute of Medical Physics and Biophysics (CC2), Charité Medical University
Jana Selent: Research Programme on Biomedical Informatics, Pompeu Fabra University, Hospital del Mar Medical Research Institute
Martha E Sommer: Institute of Medical Physics and Biophysics (CC2), Charité Medical University

Nature Communications, 2017, vol. 8, issue 1, 1-12

Abstract: Abstract G-protein-coupled receptors are membrane proteins that are regulated by a small family of arrestin proteins. During formation of the arrestin–receptor complex, arrestin first interacts with the phosphorylated receptor C terminus in a pre-complex, which activates arrestin for tight receptor binding. Currently, little is known about the structure of the pre-complex and its transition to a high-affinity complex. Here we present molecular dynamics simulations and site-directed fluorescence experiments on arrestin-1 interactions with rhodopsin, showing that loops within the C-edge of arrestin function as a membrane anchor. Activation of arrestin by receptor-attached phosphates is necessary for C-edge engagement of the membrane, and we show that these interactions are distinct in the pre-complex and high-affinity complex in regard to their conformation and orientation. Our results expand current knowledge of C-edge structure and further illuminate the conformational transitions that occur in arrestin along the pathway to tight receptor binding.

Date: 2017
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DOI: 10.1038/ncomms14258

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