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Abstract
Due to their membrane location, G protein-coupled receptors (GPCRs) are subject to regulation by soluble and integral membrane proteins as well as membrane components, including lipids and sterols. GPCRs also undergo a variety of post-translational modifications, including palmitoylation. A recent article by Zheng et al. in BMC Cell Biology demonstrates cooperative roles for receptor palmitoylation and cholesterol binding in GPCR dimerization and G protein coupling, underlining the complex regulation of these receptors.See research article http://www.biomedcentral.com/1471-2121/13/6
Highlights
Due to their membrane location, G protein-coupled receptors (GPCRs) are subject to regulation by soluble and integral membrane proteins as well as membrane components, including lipids and sterols
The β2-adrenergic receptor (β2AR) crystalized with cholesterol molecules and a post-translationally added palmitate group from each protomer forming most of the dimer interface [3], suggesting a role for lipids and sterols, in addition to protein-protein interactions, in GPCR dimerization
GPCRs have been found to associate with both regions, and it is believed that this leads to an increased local concentration of receptors and G proteins in the laterally separated regions, increasing the efficiency of signal transduction [5]
Summary
Due to their membrane location, G protein-coupled receptors (GPCRs) are subject to regulation by soluble and integral membrane proteins as well as membrane components, including lipids and sterols. The β2-adrenergic receptor (β2AR) crystalized with cholesterol molecules and a post-translationally added palmitate group from each protomer forming most of the dimer interface [3], suggesting a role for lipids and sterols, in addition to protein-protein interactions, in GPCR dimerization.
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