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Methods Mol Biol. 2019;1947:289-302. doi: 10.1007/978-1-4939-9121-1_16.

Monitoring the Aggregation of GPCRs by Fluorescence Microscopy.

Author information

1
Département de Médecine, Faculté de Médecine et des Sciences de la Santé, Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Sherbrooke, QC, Canada.
2
Département de Pharmacologie-Physiologie, Faculté de Médecine et des Sciences de la Santé, Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Sherbrooke, QC, Canada.
3
Département de Médecine, Faculté de Médecine et des Sciences de la Santé, Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Sherbrooke, QC, Canada. jean-luc.parent@usherbrooke.ca.

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.

KEYWORDS:

Aggregation; Aggresome; GPCR; Misfolding; PROTEOSTAT®

PMID:
30969423
DOI:
10.1007/978-1-4939-9121-1_16
[Indexed for MEDLINE]

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