Methods used to study the oligomeric structure of G protein-coupled receptors

Guo, H., An, S., Ward, R. J., Yang, Y., Liu, Y., Guo, X.-X., Hao, Q. and Xu, T.-R. (2017) Methods used to study the oligomeric structure of G protein-coupled receptors. Bioscience Reports, 37(2), (doi: 10.1042/bsr20160547) (PMID:28062602) (PMCID:PMC5398257)

Abstract

G-protein coupled receptors (GPCRs), which constitute the largest family of cell surface receptors, were originally thought to function as monomers, but are now recognized as being able to act in a wide range of oligomeric states and indeed, it is known that the oligomerization state of a GPCR can modulate its pharmacology and function. A number of experimental techniques have been devised to study GPCR oligomerization including those based upon traditional biochemistry such as blue-native polyacrylamide gel-electrophoresis (BN-PAGE), co-immunoprecipitation and protein-fragment complementation assays, those based upon resonance energy transfer, fluorescence resonance energy transfer (FRET), time-resolved FRET, FRET spectrometry and bioluminescence resonance energy transfer (BRET). Those based upon microscopy such as fluorescence recovery after photo-bleaching (FRAP), total internal reflection fluorescence microscopy (TIRF), spatial intensity distribution analysis (SpIDA) and various single molecule imaging techniques. Finally with the solution of a growing number of crystal structures, X-ray crystallography must be acknowledged as an important source of discovery in this field. A different, but in many ways complementary approach to the use of more traditional experimental techniques, are those involving computational methods which possess obvious merit in the study of the dynamics of oligomer formation and function. Here we summarize the latest developments which have been made in the methods used to study GPCR oligomerization and give an overview of their application.

• Item Type: Articles
• Additional Information: This study was supported by NSFC funding (81473342, 81460417, U1302225, 81460253) and High-End Talent Grant of Yunnan Province, China (2012HA008).
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Ward, Dr Richard
• Authors: Guo, H., An, S., Ward, R. J., Yang, Y., Liu, Y., Guo, X.-X., Hao, Q., and Xu, T.-R.
• College/School: College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
• Journal Name: Bioscience Reports
• Publisher: Portland Press Ltd.
• ISSN: 0144-8463
• ISSN (Online): 1573-4935
• Published Online: 06 January 2017
• Copyright Holders: Copyright © 2017 The Authors
• First Published: First published in Bioscience Reports 37(2): BSR20160547
• Publisher Policy: Reproduced in accordance with the publisher copyright policy