G-protein coupled receptors, cholesterol and palmitoylation: facts about fats. Export

@article{citeulike:3908445, 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.}, author = {Chini, Bice and Parenti, Marco}, citeulike-article-id = {3908445}, citeulike-linkout-0 = {http://dx.doi.org/10.1677/JME-08-0114}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/19131499}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=19131499}, day = {8}, doi = {10.1677/JME-08-0114}, issn = {1479-6813}, journal = {Journal of molecular endocrinology}, keywords = {cholesterol, cterm, gpcr, helix8, membrane}, month = {January}, posted-at = {2009-01-19 13:54:55}, priority = {2}, title = {G-protein coupled receptors, cholesterol and palmitoylation: facts about fats.}, url = {http://dx.doi.org/10.1677/JME-08-0114}, year = {2009} }

TY - JOUR ID - citeulike:3908445 L3 - citeulike-article-id:3908445 N2 - 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. JF - Journal of molecular endocrinology SN - 1479-6813 TI - G-protein coupled receptors, cholesterol and palmitoylation: facts about fats. KW - cholesterol KW - cterm KW - gpcr KW - helix8 KW - membrane AU - Chini, Bice AU - Parenti, Marco PY - 2009/01/08/ UR - http://dx.doi.org/10.1677/JME-08-0114 ER -