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Nat Commun. 2017 Feb 21;8:14258. doi: 10.1038/ncomms14258.

C-edge loops of arrestin function as a membrane anchor.

Author information

1
Institute of Medical Physics and Biophysics (CC2), Charité Medical University, Charitéplatz 1, Berlin 10117, Germany.
2
Research Programme on Biomedical Informatics, Department of Experimental and Health Sciences, Pompeu Fabra University, Hospital del Mar Medical Research Institute, Carrer del Dr. Aiguader, 88, Barcelona 08003, Spain.

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.

PMID:
28220785
PMCID:
PMC5321764
DOI:
10.1038/ncomms14258
[Indexed for MEDLINE]
Free PMC Article

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