It has become increasingly apparent that some G protein-coupled receptors (GPCRs) are not homogeneously expressed within the plasma membrane but may instead be organised within distinct signalling microdomains. These microdomains localise GPCRs in close proximity with other membrane proteins and intracellular signalling partners and could have profound implications for the spatial and temporal control of downstream signalling. In order to probe the molecular mechanisms that govern GPCR pharmacology within these domains, fluorescence techniques with effective single receptor sensitivity are required. Of these, fluorescence correlation spectroscopy (FCS) is a technique that meets this sensitivity threshold. This short review will provide an update of the recent uses of FCS based techniques in conjunction with GPCR subtype selective fluorescent ligands to characterise dynamic ligand–receptor interactions in whole cells and using purified GPCRs.
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Glycoproteomics is the tool of choice in glycobiology to decipher the role of protein glycosylation in health and disease in a system-wide context for integration into multi-omics studies. For a hitchhiker's guide to glcoproteomics, see the review by Oliveira and colleagues (pp. 1623–1642). Cover artwork provided by Daniel Kolarich.
The use of fluorescence correlation spectroscopy to characterise the molecular mobility of G protein-coupled receptors in membrane microdomains: an update Available to Purchase
Laura E. Kilpatrick, Stephen J. Hill; The use of fluorescence correlation spectroscopy to characterise the molecular mobility of G protein-coupled receptors in membrane microdomains: an update. Biochem Soc Trans 27 August 2021; 49 (4): 1547–1554. doi: https://doi.org/10.1042/BST20201001
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