Defining the functional equivalence of wild-type and chemically engineered G protein-coupled receptors

Alvarez-Curto, E. and Milligan, G. (2015) Defining the functional equivalence of wild-type and chemically engineered G protein-coupled receptors. In: Thiel, G. (ed.) Designer Receptors Exclusively Activated by Designer Drugs. Series: Neuromethods (108). Springer New York, pp. 1-28. ISBN 9781493929436 (doi:10.1007/978-1-4939-2944-3_1)

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Abstract

The functional connection between activation of a single G protein-coupled receptor (GPCR) and a specific physiological outcome may be obscured by the presence of other closely related members of the GPCR superfamily that share spatiotemporal patterns of expression and equipotent activation by endogenous ligands. To address this issue, molecular and chemical genetic techniques have been developed to generate mutationally modified GPCRs only susceptible to activation by one or more synthetic ligands that are inactive at the equivalent wild-type receptor. This chapter provides both an overview of strategies used to generate such “receptors activated solely by synthetic ligands” (RASSLs) and, in more detail, approaches that have been used to assess the equivalence or otherwise of function of a wild-type and corresponding RASSL receptor. The human muscarinic M3 acetylcholine receptor is used as the exemplar but similar preliminary studies should be employed before further use, particularly in vivo, of such RASSLs.

Item Type:Book Sections
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Milligan, Professor Graeme and Alvarez-Curto, Dr Elisa
Authors: Alvarez-Curto, E., and Milligan, G.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Publisher:Springer New York
ISSN:0893-2336
ISBN:9781493929436

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