Abstract
G protein-coupled receptors (GPCRs) are the largest class of molecules involved in signal transduction across cell membranes and are major drug targets. Since GPCRs are integral membrane proteins, their structure and function are modulated by membrane lipids. In particular, membrane cholesterol is an important lipid in the context of GPCR function. Solubilization of integral membrane proteins is a process in which the proteins and lipids in native membranes are dissociated in the presence of a suitable amphiphilic detergent. Interestingly, solubilization offers a convenient approach to monitor lipid-receptor interaction as it results in differential extents of lipid solubilization, thereby allowing to assess the role of specific lipids on receptor function. In this review, we highlight how this solubilization strategy is utilized to decipher novel information about the structural stringency of cholesterol necessary for supporting the function of the serotonin(1A) receptor. We envision that insight in GPCR-lipid interaction would result in better understanding of GPCR function in health and disease.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
