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Diffusion and Oligomerization States of the Muscarinic M Receptor in Live Cells─The Impact of Ligands and Membrane Disruptors. | LitMetric

AI Article Synopsis

Article Abstract

G protein-coupled receptors (GPCRs) are a major gateway to cellular signaling, which respond to ligands binding at extracellular sites through allosteric conformational changes that modulate their interactions with G proteins and arrestins at intracellular sites. High-resolution structures in different ligand states, together with spectroscopic studies and molecular dynamics simulations, have revealed a rich conformational landscape of GPCRs. However, their supramolecular structure and spatiotemporal distribution is also thought to play a significant role in receptor activation and signaling bias within the native cell membrane environment. Here, we applied single-molecule fluorescence techniques, including single-particle tracking, single-molecule photobleaching, and fluorescence correlation spectroscopy, to characterize the diffusion and oligomerization behavior of the muscarinic M receptor (MR) in live cells. Control samples included the monomeric protein CD86 and fixed cells, and experiments performed in the presence of different orthosteric MR ligands and of several compounds known to change the fluidity and organization of the lipid bilayer. M receptors exhibit Brownian diffusion characterized by three diffusion constants: (∼0.01 μm/s), (∼0.04 μm/s), and (∼0.14 μm/s), whose populations were found to be modulated by both orthosteric ligands and membrane disruptors. The lipid raft disruptor C6 ceramide led to significant changes for CD86, while the diffusion of MR remained unchanged, indicating that M receptors do not partition in lipid rafts. The extent of receptor oligomerization was found to be promoted by increasing the level of expression and the binding of orthosteric ligands; in particular, the agonist carbachol elicited a large increase in the fraction of MR oligomers. This study provides new insights into the balance between conformational and environmental factors that define the movement and oligomerization states of GPCRs in live cells under close-to-native conditions.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11090110PMC
http://dx.doi.org/10.1021/acs.jpcb.4c01035DOI Listing

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