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Assays for detecting arrestin interaction with GPCRs.

Nicole A Perry-Hauser¹, Wesley B Asher², Maria Hauge Pedersen³

¹Department of Psychiatry, Columbia University, Vagelos College of Physicians and Surgeons, New York, NY, United States; Division of Molecular Therapeutics, New York Psychiatric Institute, New York, NY, United States.

Methods in Cell Biology

|November 9, 2021

Summary

Arrestin proteins are crucial for G protein-coupled receptor (GPCR) regulation and signaling. Assays measuring arrestin binding to GPCRs are vital for drug discovery, with new methods offering receptor-independent analysis.

Keywords:

Arrestin Cell signaling G protein-coupled receptors (GPCRs)Unmodified receptor

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Area of Science:

Biochemistry
Molecular Pharmacology
Cell Biology

Background:

Vertebrate arrestins regulate G protein-coupled receptor (GPCR) desensitization, internalization, and signaling.
Biased arrestin versus G protein signaling holds therapeutic potential, necessitating robust assays for drug discovery.

Purpose of the Study:

To review techniques for measuring arrestin binding to GPCRs.
To provide an in-depth methodological review of two receptor-modification-free assays for arrestin-GPCR interactions.

Main Methods:

Review of established arrestin-GPCR binding assays.
Detailed examination of two novel methods: direct binding assay (purified arrestin and rhodopsin) and a living-cell recruitment assay.

Main Results:

Established methods for measuring arrestin binding to GPCRs were summarized.
Two receptor-modification-free methods were detailed, focusing on direct binding and cellular recruitment.

Conclusions:

Accurate measurement of arrestin-GPCR interactions is critical for drug discovery.
The presented receptor-modification-free methods offer valuable tools for studying arrestin bias and GPCR signaling pathways.