Detection and quantitative analysis of dynamic GPCRs interactions using flow cytometry-based FRET

  • Barbara Chruścicka
  • , Shauna E. Wallace Fitzsimons
  • , Clémentine M. Druelle
  • , Timothy G. Dinan
  • , Harriët Schellekens

Research output: Chapter in Book/Report/Conference proceedingsChapterpeer-review

Abstract

Heterodimerization of specific G protein-coupled receptor (GPCR) protomers is associated with increased receptor signaling diversity and exhibits unique biochemical, functional, and pharmacological properties. Evidence for the formation of heteroreceptor complexes has been demonstrated in vitro using cellular models and biochemical assays and ex vivo using brain slices and primary cell cultures. Since mechanisms that lead to brain pathologies such as depression, anxiety, addiction, and schizophrenia involve GPCR signaling, the distinct pharmacological profiles of GPCR assemblies may serve as new target for the development of novel therapeutic strategies with enhanced specificity. Therefore, development and standardization of novel methods for detection and analysis of dimer pairs both in recombinant systems and in native tissue is warranted. This chapter describes a step-by-step protocol for detecting and quantifying dynamic receptor–receptor interactions in living cells using flow cytometry-based fluorescence (Förster) resonance energy transfer (fcFRET). This method has significant potential to identify novel GPCR dimers within the central nervous system while simultaneously allowing analysis of the dynamic nature of these receptor interactions, which is poised to contribute significantly to the field of GPCR neuropsychopharmacology across brain diseases.

Original languageEnglish
Title of host publicationNeuromethods
PublisherHumana Press Inc.
Pages223-238
Number of pages16
DOIs
Publication statusPublished - 2018

Publication series

NameNeuromethods
Volume140
ISSN (Print)0893-2336
ISSN (Electronic)1940-6045

Keywords

  • Dimerization
  • Flow cytometry
  • Fluorescent resonance energy transfer
  • G protein-coupled receptors
  • Heteroreceptor complexes
  • Receptor–receptor interactions

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