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This Article Accepted manuscript (PDF) All Versions of this Article: JME-08-0114v1 42/5/371    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Chini, B. Articles by Parenti, M. Search for Related Content PubMed PubMed Citation Articles by Chini, B. Articles by Parenti, M.

B Chini, Cellular and Molecular Pharmacology Section, CNR Institute of Neuroscience, 20129, Italy
M Parenti, Department of Experimental Medicine, University of Milano-Bicocca, Monza, Italy

Correspondence: Bice Chini, Email: b.chini{at}in.cnr.it

Abstract

G protein-coupled receptors are integral membrane proteins, hence it is not a big surprise that a number of their structural and functional features are modulated both by proteins and lipids. The impact of interacting proteins and lipids on the assembly and signalling of GPCRs have been extensively investigated over the last 20-30 years, and a further impetus has been given by the proposal that GPCRs and/or their immediate signalling partners (G proteins) can partition within plasma membrane domains, termed rafts and caveolae, enriched in glycosphingolipids and cholesterol. The high content of these specific lipids, in particular of cholesterol, in the vicinity of GPCR transmembranes can affect GPCR structure and/or function. In addition, most GPCRs are post-translationally modified with one or more palmitic acid(s), a 16-carbon saturated fatty acid, covalently bound to cysteine(s) localized in the carboxyl-terminal cytoplasmic tail. The insertion of palmitate into the cytoplasmic leaflet of the plasma membrane can create a fourth loop, thus profoundly affecting GPCR structure and hence the interactions with intracellular partner proteins. This review briefly highlights how lipids of the membrane and of receptor themselves can influence GPCR organisation and functioning.