ArticleThe Journal of biological chemistry2010
Oligomeric size of the m2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 74 citations in OpenAlex.
- Precise Alternation Between Image-Forming Sample Planes Enables Quantitative Monitoring of Receptor-Arrestin Interaction Dynamics at the Plasma Membrane of Live Cells.bioRxiv : the preprint server for biology · 2026Article
- Distinct membrane binding properties of the two non-visual arrestins.Communications biology · 2026Article
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- ATP8A1-translocated endosomal phosphatidylserine fine-tunes the multivesicular body formation and the endo-lysosomal traffic.iScience · 2025Article
- Diffusion and Oligomerization States of the Muscarinic MThe journal of physical chemistry. B · 2024Article
- The MProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Live-cell microscopy or fluorescence anisotropy with budded baculoviruses-which way to go with measuring ligand binding to MOpen biology · 2022Article
- Allostery of atypical modulators at oligomeric G protein-coupled receptors.Scientific reports · 2021Article
- Determination of G-protein-coupled receptor oligomerization by molecular brightness analyses in single cells.Nature protocols · 2021Article
- Ligand-Induced Coupling between Oligomers of the MBiophysical journal · 2018Article
- Muscarinic receptor oligomerization.Neuropharmacology · 2018Review
- Spatial Intensity Distribution Analysis: Studies of G Protein-Coupled Receptor Oligomerisation.Trends in pharmacological sciences · 2018Review
- An intermolecular FRET sensor detects the dynamics of T cell receptor clustering.Nature communications · 2017Article
- Article
- Unraveling a molecular determinant for clathrin-independent internalization of the M2 muscarinic acetylcholine receptor.Scientific reports · 2015Article
- Distinct Agonist Regulation of Muscarinic Acetylcholine M2-M3 Heteromers and Their Corresponding Homomers.The Journal of biological chemistry · 2015Article
- Experimental verification of the kinetic theory of FRET using optical microspectroscopy and obligate oligomers.Biophysical journal · 2015Article
- The sigma-1 receptors are present in monomeric and oligomeric forms in living cells in the presence and absence of ligands.The Biochemical journal · 2015Article
- Coupling of g proteins to reconstituted monomers and tetramers of the M2 muscarinic receptor.The Journal of biological chemistry · 2014Article
- Watching single proteins using engineered nanopores.Protein and peptide letters · 2014Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Fluorescence resonance energy transfer (FRET), measured by fluorescence intensity-based microscopy and fluorescence lifetime imaging, has been used to estimate the size of oligomers formed by the M(2) muscarinic cholinergic receptor. The approach is based on the relationship between the apparent FRET efficiency within an oligomer of specified size (n) and the pairwise FRET efficiency between a single donor and a single acceptor (E). The M(2) receptor was fused at the N terminus to enhanced green or yellow fluorescent protein and expressed in Chinese hamster ovary cells. Emission spectra were analyzed by spectral deconvolution, and apparent efficiencies were estimated by donor-dequenching and acceptor-sensitized emission at different ratios of enhanced yellow fluorescent protein-M(2) receptor to enhanced green fluorescent protein-M(2) receptor. The data were interpreted in terms of a model that considers all combinations of donor and acceptor within a specified oligomer to obtain fitted values of E as follows: n = 2, 0.495 +/- 0.019; n = 4, 0.202 +/- 0.010; n = 6, 0.128 +/- 0.006; n = 8, 0.093 +/- 0.005. The pairwise FRET efficiency determined independently by fluorescence lifetime imaging was 0.20-0.24, identifying the M(2) receptor as a tetramer. The strategy described here yields an explicit estimate of oligomeric size on the basis of fluorescence properties alone. Its broader application could resolve the general question of whether G protein-coupled receptors exist as dimers or larger oligomers. The size of an oligomer has functional implications, and such information can be expected to contribute to an understanding of the signaling process.
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Registered trials
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