G protein-coupled receptors (GPCRs) comprise the largest family of integral membrane proteins, which are coupled to heterotrimeric G proteins to influence cell signaling. Subsequent to G protein activation, agonist-stimulated G protein-coupled receptor kinase (GRK) phosphorylation results in the recruitment of β-arrestin proteins, which form both stable and unstable complexes with GPCRs. β-Arrestins when bound to GPCRs not only contribute to the uncoupling of G protein signaling but also to the redistribution of GPCRs to clathrin-coated pits via their association with both clathrin and β2-adaptin facilitating GPCR endocytosis. This allows β-arrestins to couple GPCRs to additional cell signaling proteins allowing a second wave of receptor signaling. Importantly, the β-arrestin-regulated subcellular localization of these complexes also plays a critical role in regulating how these signals are transduced and which proteins are recruited. Here, we describe a methodology for assessing the GPCR subcellular localization by super-resolution microscopy and suggest that this methodology can be extended to the study of GPCR/protein complexes.
CITATION STYLE
Caetano Crowley, F. A., Heit, B., & Ferguson, S. S. G. (2019). Super-Resolution Imaging of G Protein-Coupled Receptors Using Ground State Depletion Microscopy. In Methods in Molecular Biology (Vol. 1947, pp. 323–336). Humana Press Inc. https://doi.org/10.1007/978-1-4939-9121-1_18
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