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The human neurotensin receptor 1 (NTSR1) is a G protein-coupled receptor. Thereceptor is activated by a small peptide ligand neurotensin. NTSR1 can beexpressed in HEK cells by stable transfection. Previously we used thefluorescent protein markers mRuby3 or mNeonGreen fused to NTSR1 for EMCCD-basedstructured illumination microscopy (SIM) in living HEK cells. Ligand bindinginduced conformational changes in NTSR1 which triggered the intracellularsignaling processes. Recent single-molecule studies revealed a dynamicmonomer/dimer equilibrium of this receptor in artificial lipid bilayers. Herewe report on the oligomerization state of human NTSR1 from living cells bytrapping them into lipid nanodiscs. Briefly, SMALPs (styrene-maleic acidcopolymer lipid nanoparticles) were produced directly from the plasma membranesof living HEK293T FlpIn cells. SMALPs with a diameter of 15 nm were soluble andstable. NTSR1 in SMALPs were analyzed by single-molecule intensity measurementsone membrane patch at a time using a custom-built confocal anti-Brownianelectrokinetic trap (ABEL trap) microscope. We found oligomerization changesbefore and after stimulation of the receptor with its ligand neurotensin.

Monitoring oligomerization dynamics of individual human neurotensin receptors 1 in living cells and in SMALP nanodiscs