β-Arrestin biosensors reveal a rapid, receptor-dependent activation/deactivation cycle

Susanne Nuber, Ulrike Zabel, Kristina Lorenz, Andreas Nuber, Graeme Milligan, Andrew B. Tobin, Martin J. Lohse () and Carsten Hoffmann ()
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Susanne Nuber: Institute of Pharmacology and Toxicology, University of Würzburg
Ulrike Zabel: Institute of Pharmacology and Toxicology, University of Würzburg
Kristina Lorenz: Institute of Pharmacology and Toxicology, University of Würzburg
Andreas Nuber: Institute of Pharmacology and Toxicology, University of Würzburg
Graeme Milligan: Molecular Pharmacology Group, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow
Andrew B. Tobin: MRC Toxicology Unit, University of Leicester
Martin J. Lohse: Institute of Pharmacology and Toxicology, University of Würzburg
Carsten Hoffmann: Institute of Pharmacology and Toxicology, University of Würzburg

Nature, 2016, vol. 531, issue 7596, 661-664

Abstract: A series of FRET-based β-arrestin2 biosensors are used to study the dynamics and conformational changes that occur when β-arrestin2 binds to and dissociates from the β2-adrenergic receptor in living cells; results show that after β-arrestin2 dissociates from the β2-adrenergic receptor, it stays at the cell membrane in an active conformation for a while, indicating that β-arrestin is able to signal in a G-protein-coupled receptor (GPCR)-free state.

Date: 2016
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DOI: 10.1038/nature17198

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