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Monitoring the Aggregation of GPCRs by Fluorescence Microscopy

  • Samuel Génier
  • Jade Degrandmaison
  • Christine L. Lavoie
  • Louis Gendron
  • Jean-Luc ParentEmail author
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1947)

Abstract

G protein-coupled receptors (GPCRs) contain highly hydrophobic domains that are subject to aggregation when exposed to the crowded environment of the cytoplasm. Many events can lead to protein aggregation such as mutations, endoplasmic reticulum (ER) stress, and misfolding. These processes have been widely known to impact GPCR folding, maturation, and localization. Protein aggregates are transported toward the microtubule-organizing center via dynein to form a large juxta-nuclear structure called the aggresome, and in due course, are then targeted for degradation. Here, we describe a method to study aggregation of GPCRs by fluorescence microscopy.

Key words

GPCR Aggregation Aggresome Misfolding PROTEOSTAT® 

Notes

Acknowledgments

This work was supported by a grant from the Natural Sciences and Engineering Research Council of Canada and by the André-Lussier Research chair to J.-L.P, and by Ph.D. scholarships from NSERC (S.G.) and from the Fonds de Recherche du Québec-Santé (S.G. and J.D.). The authors are grateful to Leonid Volkov for his expertise in confocal microscopy.

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • Samuel Génier
    • 1
  • Jade Degrandmaison
    • 1
  • Christine L. Lavoie
    • 2
  • Louis Gendron
    • 2
  • Jean-Luc Parent
    • 1
    Email author
  1. 1.Département de Médecine, Faculté de Médecine et des Sciences de la Santé, Institut de Pharmacologie de SherbrookeUniversité de SherbrookeSherbrookeCanada
  2. 2.Département de Pharmacologie-Physiologie, Faculté de Médecine et des Sciences de la Santé, Institut de Pharmacologie de SherbrookeUniversité de SherbrookeSherbrookeCanada

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