English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Plus

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Zendy Tools

Zendy Open

G protein-coupled receptors (GPCRs) are a large superfamily of membraneproteins that are activated by extracellular small molecules or photons.Neurotensin receptor 1 (NTSR1) is a GPCR that is activated by neurotensin, i.e.a 13 amino acid peptide. Binding of neurotensin induces conformational changesin the receptor that trigger the intracellular signaling processes. Whilerecent single-molecule studies have reported a dynamic monomer - dimerequilibrium of NTSR1 in vitro, a biophysical characterization of theoligomerization status of NTSR1 in living mammalian cells is complicated. Herewe report on the oligomerization state of the human NTSR1 tagged with mRuby3 bydissolving the plasma membranes of living HEK293T cells into 10 nm-sizedsoluble lipid nanoparticles by addition of styrene-maleic acid copolymers(SMALPs). Single SMALPs were analyzed one after another in solution bymulti-parameter single molecule spectroscopy including brightness, fluorescencelifetime and anisotropy for homoFRET. Brightness analysis was improved usingsingle SMALP detection in a confocal ABELtrap for extended observation times insolution. A bimodal brightness distribution indicated a significant fraction ofdimeric NTSR1 in SMALPs or in the plasma membrane, respectively, beforeaddition of neurotensin.

Observing monomer - dimer transitions of neurotensin receptors 1 in single SMALPs by homoFRET and in an ABELtrap