ArticleThe Biochemical journal2016
Quaternary structures of opsin in live cells revealed by FRET spectrometry.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 52 citations in OpenAlex.
- Mechanistic insights from the atomic-level quaternary structure of short-lived GPCR oligomers of the human secretin receptor in live cells.Communications biology · 2025Article
- Mechanistic insights from the atomic-level quaternary structure of short-lived GPCR oligomers in live cells.Research square · 2024Article
- Implementation of FRET Spectrometry Using Temporally Resolved Fluorescence: A Feasibility Study.International journal of molecular sciences · 2024Article
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- G Protein-Dependent Activation of the PKA-Erk1/2 Pathway by the Striatal Dopamine D1/D3 Receptor Heteromer Involves Beta-Arrestin and the Tyrosine Phosphatase Shp-2.Biomolecules · 2023Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021Review
- Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021Review
- Fluorescence intensity fluctuation analysis of receptor oligomerization in membrane domains.Biophysical journal · 2021Article
- Article
- Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019Review
- Cryo-EM structure of the native rhodopsin dimer in nanodiscs.The Journal of biological chemistry · 2019Article
- A general method to quantify ligand-driven oligomerization from fluorescence-based images.Nature methods · 2019Article
- Ab Initio Derivation of the FRET Equations Resolves Old Puzzles and Suggests Measurement Strategies.Biophysical journal · 2019Article
- Regulation of G protein-coupled receptor signaling by plasma membrane organization and endocytosis.Traffic (Copenhagen, Denmark) · 2019Review
- Raftophilic rhodopsin-clusters offer stochastic platforms for G protein signalling in retinal discs.Communications biology · 2019Article
- Asymmetric Recruitment of β-Arrestin1/2 by the Angiotensin II Type I and Prostaglandin F2α Receptor Dimer.Frontiers in endocrinology · 2019Article
- Investigating the Nanodomain Organization of Rhodopsin in Native Membranes by Atomic Force Microscopy.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Detection of misfolded rhodopsin aggregates in cells by Förster resonance energy transfer.Methods in cell biology · 2019Article
- New Techniques to Study Intracellular Receptors in Living Cells: Insights Into RIG-I-Like Receptor Signaling.Advances in experimental medicine and biology · 2019Review
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Rhodopsin is a prototypical G-protein-coupled receptor (GPCR) that initiates phototransduction in the retina. The receptor consists of the apoprotein opsin covalently linked to the inverse agonist 11-cis retinal. Rhodopsin and opsin have been shown to form oligomers within the outer segment disc membranes of rod photoreceptor cells. However, the physiological relevance of the observed oligomers has been questioned since observations were made on samples prepared from the retina at low temperatures. To investigate the oligomeric status of opsin in live cells at body temperatures, we utilized a novel approach called Förster resonance energy transfer spectrometry, which previously has allowed the determination of the stoichiometry and geometry (i.e. quaternary structure) of various GPCRs. In the current study, we have extended the method to additionally determine whether or not a mixture of oligomeric forms of opsin exists and in what proportion. The application of this improved method revealed that opsin expressed in live Chinese hamster ovary (CHO) cells at 37°C exists as oligomers of various sizes. At lower concentrations, opsin existed in an equilibrium of dimers and tetramers. The tetramers were in the shape of a near-rhombus. At higher concentrations of the receptor, higher-order oligomers began to form. Thus, a mixture of different oligomeric forms of opsin is present in the membrane of live CHO cells and oligomerization occurs in a concentration-dependent manner. The general principles underlying the concentration-dependent oligomerization of opsin may be universal and apply to other GPCRs as well.
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