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Current Medicinal Chemistry


ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

GPR55 and its Interaction with Membrane Lipids: Comparison with Other Endocannabinoid-Binding Receptors

Author(s): V. Gasperi, E. Dainese, S. Oddi, A. Sabatucci and M. Maccarrone

Volume 20 , Issue 1 , 2013

Page: [64 - 78] Pages: 15

DOI: 10.2174/0929867311302010008

Price: $65


A number of integral membrane G protein-coupled receptors (GPCRs) share common structural features (including palmytoilated aminoacid residues and consensus sequences specific for interaction with cholesterol) that allow them to interact with lipid rafts, membrane cholesterol-rich microdomains able to regulate GPCR signalling and functions. Among GPCRs, type-1 and type-2 cannabinoid receptors, the molecular targets of endocannabinoids (eCBs), control many physiological and pathological processes through the activation of several signal transduction pathways. Recently, the orphan GPR55 receptor has been proved to be activated by many eCBs, thus leading to the hypothesis that it might be the “type-3” cannabinoid receptor. While the biological activity of eCBs and the influence of membrane lipids on their functions are rather well established, information regarding GPR55 is still scarce and often controversial. Based on this background, here we shall review current data about GPR55 pharmacology and signalling, highlighting its involvement in several pathophysiological conditions. We shall also outline the structural features that allow GPR55 to interact with cholesterol and to associate with lipid rafts; how the latter lipid microdomains impact the biological activity of GPR55 is also addressed, as well as their potential for the discovery of new therapeutics useful for the treatment of those human diseases that might be associated with alterations of GPR55 activity.

Keywords: Cannabinoid receptors, cholesterol, endocannabinoids, GPR55, lipid rafts, plasma membranes, integral membrane, G protein-coupled receptors (GPCRs), aminoacid residues, consensus sequences

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