Methods to monitor the quaternary structure of G protein-coupled receptors.
A wide range of approaches has been applied to examine the quaternary structure of G protein-coupled receptors, the basis of such protein-protein interactions and how such interactions might modulate the pharmacology and function of these receptors. These include co-immunoprecipitation, various adaptations of resonance energy transfer techniques, functional complementation studies and the analysis of ligand-binding data. Each of the available techniques has limitations that restrict interpretation of the data. However, taken together, they provide a coherent body of evidence indicating that many, if not all, G protein-coupled receptors exist and function as dimer/oligomers. Herein we assess the widely applied techniques and discuss the relative benefits and limitations of these approaches.
Milligan
Graeme
G
Molecular Pharmacology Group, Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, UK.
Bouvier
Michel
M
D000818:Animals; D001671:Biochemistry / Q000379:methods; D019281:Dimerization; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D006801:Humans; D047468:Immunoprecipitation / Q000379:methods; D008024:Ligands; D008163:Luminescent Measurements / Q000379:methods; D008967:Molecular Biology / Q000379:methods*; D020836:Protein Structure, Quaternary; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry* / Q000378:metabolism
D008024:Ligands; D043562:Receptors, G-Protein-Coupled