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Probing Arrestin Function Using Intramolecular FlAsH-BRET Biosensors.

Erik G Strungs1, Louis M Luttrell2,3, Mi-Hye Lee1

  • 1Department of Medicine, Medical University of South Carolina, Charleston, SC, USA.

Methods in Molecular Biology (Clifton, N.J.)
|March 29, 2019
PubMed
Summary
This summary is machine-generated.

This study introduces a novel biosensor to track changes in arrestin conformation within live cells. This method reveals how G protein-coupled receptor (GPCR) and ligand structures dictate cellular signaling pathways.

Keywords:
ArrestinBioluminescence resonance energy transfer (BRET)Fluorescent arsenicalG protein-coupled receptor (GPCR)Ligand efficacySignal transduction

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Pharmacology

Background:

  • G protein-coupled receptors (GPCRs) mediate cellular responses to extracellular signals.
  • Ligand binding to GPCRs induces conformational changes, influencing downstream signaling via effectors like arrestins.
  • Understanding these conformational dynamics is crucial for deciphering signal transduction pathways.

Purpose of the Study:

  • To develop and validate a novel biosensor for measuring stimulus-induced conformational changes in arrestin proteins.
  • To investigate how GPCR and ligand structures influence arrestin conformation and activation modes.
  • To establish a method for classifying GPCRs and ligands based on their distinct arrestin activation signatures.

Main Methods:

  • Utilized intramolecular fluorescein arsenical hairpin (FlAsH) bioluminescence resonance energy transfer (BRET) biosensors.
  • Engineered Rluc-arrestin3-FlAsH-BRET constructs with N-terminal Renilla luciferase donors and tetracysteine-tagged arrestin3.
  • Measured changes in net BRET in live cells upon GPCR stimulation from multiple vantage points within arrestin3.

Main Results:

  • Successfully measured stimulus-induced conformational changes in arrestin3 using the developed BRET biosensors.
  • Demonstrated that GPCR and ligand structures imprint distinct conformational signatures onto arrestin3.
  • Showcased the ability to differentiate arrestin3 activation modes based on receptor-ligand interactions.

Conclusions:

  • The Rluc-arrestin3-FlAsH-BRET biosensor provides a powerful tool for real-time monitoring of arrestin conformation.
  • This approach elucidates the intricate mechanisms of information transfer across the plasma membrane mediated by GPCRs.
  • The findings enable classification of GPCRs and ligands by their unique effects on arrestin activation, advancing drug discovery and signaling research.