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C-edge loops of arrestin function as a membrane anchor

Author

Listed:
  • 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)

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.

Suggested Citation

  • Ciara C M. Lally & Brian Bauer & Jana Selent & Martha E Sommer, 2017. "C-edge loops of arrestin function as a membrane anchor," Nature Communications, Nature, vol. 8(1), pages 1-12, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14258
    DOI: 10.1038/ncomms14258
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    Cited by:

    1. Raphael S. Haider & Edda S. F. Matthees & Julia Drube & Mona Reichel & Ulrike Zabel & Asuka Inoue & Andy Chevigné & Cornelius Krasel & Xavier Deupi & Carsten Hoffmann, 2022. "β-arrestin1 and 2 exhibit distinct phosphorylation-dependent conformations when coupling to the same GPCR in living cells," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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