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

Author

Listed:
  • Susanne Nuber

    (Institute of Pharmacology and Toxicology, University of Würzburg
    Rudolf Virchow Center, University of Würzburg)

  • Ulrike Zabel

    (Institute of Pharmacology and Toxicology, University of Würzburg
    Rudolf Virchow Center, University of Würzburg)

  • Kristina Lorenz

    (Institute of Pharmacology and Toxicology, University of Würzburg
    Comprehensive Heart Failure Center, University of Würzburg
    †Present address: Leibniz Institute for Analytical Sciences ISAS, Bunsen-Kirchhoff-Str. 11, 44139 Dortmund, Germany (K.L.); Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13092 Berlin, Germany (M.J.L.).)

  • 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
    Rudolf Virchow Center, University of Würzburg
    Comprehensive Heart Failure Center, University of Würzburg
    †Present address: Leibniz Institute for Analytical Sciences ISAS, Bunsen-Kirchhoff-Str. 11, 44139 Dortmund, Germany (K.L.); Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13092 Berlin, Germany (M.J.L.).)

  • Carsten Hoffmann

    (Institute of Pharmacology and Toxicology, University of Würzburg
    Rudolf Virchow Center, University of Würzburg)

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.

Suggested Citation

  • Susanne Nuber & Ulrike Zabel & Kristina Lorenz & Andreas Nuber & Graeme Milligan & Andrew B. Tobin & Martin J. Lohse & Carsten Hoffmann, 2016. "β-Arrestin biosensors reveal a rapid, receptor-dependent activation/deactivation cycle," Nature, Nature, vol. 531(7596), pages 661-664, March.
    • Handle: RePEc:nat:nature:v:531:y:2016:i:7596:d:10.1038_nature17198
    DOI: 10.1038/nature17198
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