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The conformational signature of β-arrestin2 predicts its trafficking and signalling functions

Author

Listed:
  • Mi-Hye Lee

    (Medical University of South Carolina)

  • Kathryn M. Appleton

    (Medical University of South Carolina)

  • Erik G. Strungs

    (Medical University of South Carolina)

  • Joshua Y. Kwon

    (Medical University of South Carolina)

  • Thomas A. Morinelli

    (Medical University of South Carolina)

  • Yuri K. Peterson

    (College of Pharmacy, Medical University of South Carolina)

  • Stephane A. Laporte

    (McGill University Health Center Research Institute, McGill University
    Pharmacology and Therapeutics, McGill University
    Anatomy and Cell Biology, McGill University)

  • Louis M. Luttrell

    (Medical University of South Carolina
    Research Service of the Ralph H. Johnson Veterans Affairs Medical Center)

Abstract

A series of intramolecular fluorescent FlAsH BRET reporters is used to monitor conformational changes in β-arrestin2 following activation of seven G-protein-coupled receptors (GPCRs), showing that different GPCRs produce distinct β-arrestin2 conformational signatures that correlate with the stability of the receptor–arrestin complex and the role of β-arrestin2 in activating or dampening downstream signalling events, which explains how different GPCRs can use a common effector for different purposes.

Suggested Citation

  • Mi-Hye Lee & Kathryn M. Appleton & Erik G. Strungs & Joshua Y. Kwon & Thomas A. Morinelli & Yuri K. Peterson & Stephane A. Laporte & Louis M. Luttrell, 2016. "The conformational signature of β-arrestin2 predicts its trafficking and signalling functions," Nature, Nature, vol. 531(7596), pages 665-668, March.
    • Handle: RePEc:nat:nature:v:531:y:2016:i:7596:d:10.1038_nature17154
    DOI: 10.1038/nature17154
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