ArticleBiophysical journal2013
The 5-HT3AB receptor shows an A3B2 stoichiometry at the plasma membrane.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- The serotonin-gated 5-HT3 receptor: a tale of functions and structures of a prototypical pentameric ligand-gated ion channel.Acta pharmacologica Sinica · 2026Review
- Predicted conformations of 5-HT3 receptor ion channels are modified by subunit D.Computational and structural biotechnology journal · 2025Article
- Article
- VHH Nanobody Versatility against Pentameric Ligand-Gated Ion Channels.Journal of medicinal chemistry · 2024Review
- 5-HTInternational journal of molecular sciences · 2023Article
- Article
- Tapping into 5-HTInternational journal of molecular sciences · 2021Review
- International Union of Basic and Clinical Pharmacology. CX. Classification of Receptors for 5-hydroxytryptamine; Pharmacology and Function.Pharmacological reviews · 2021Review
- Interactions of the α3β2 Nicotinic Acetylcholine Receptor Interfaces with α-Conotoxin LsIA and its Carboxylated C-terminus Analogue: Molecular Dynamics Simulations.Marine drugs · 2020Article
- Supported Cell Membrane Sheets to Monitor Protein Assembly.Bio-protocol · 2019Article
- Human-derived gut microbiota modulates colonic secretion in mice by regulating 5-HTAmerican journal of physiology. Gastrointestinal and liver physiology · 2017Article
- Novel mechanism of modulation at a ligand-gated ion channel; action of 5-Cl-indole at the 5-HTBritish journal of pharmacology · 2016Article
- Identifying the elusive link between amino acid sequence and charge selectivity in pentameric ligand-gated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Manipulation of Subunit Stoichiometry in Heteromeric Membrane Proteins.Structure (London, England : 1993) · 2016Article
- Article
- 5-HT3 Receptor Brain-Type B-Subunits are Differentially Expressed in Heterologous Systems.ACS chemical neuroscience · 2015Article
- Experimental verification of the kinetic theory of FRET using optical microspectroscopy and obligate oligomers.Biophysical journal · 2015Article
- Allosteric activation of the 5-HT3AB receptor by mCPBG.Neuropharmacology · 2015Article
- The duplicated α7 subunits assemble and form functional nicotinic receptors with the full-length α7.The Journal of biological chemistry · 2014Article
- Exploring a potential palonosetron allosteric binding site in the 5-HT(3) receptor.Bioorganic & medicinal chemistry · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
The 5-HT3AB receptor is the best-characterized heteropentameric 5-HT3 receptor. Under conditions of heterologous expression, the 5-HT3AB receptor shows a single functionally resolvable population, suggesting the presence of a unique subunit stoichiometry; however, conflicting previous reports have suggested two different possible stoichiometries. Here we isolate plasma membrane sheets containing assembled receptors from individual HEK293T cells. We then determine the stoichiometry of 5-HT3AB receptors on the plasma membrane by fluorescence methods, employing meCFP- and meYFP-labeled A and B subunits. Over a wide range of cDNA transfection ratios, fluorescence intensity ratios are closest to values that correspond to a subunit ratio of A3B2. Förster resonance energy transfer (family FRET) efficiencies provide minor corrections (3-6%) to the subunit ratios and provide independent support for a predominantly A3B2 stoichiometry on the plasma membrane sheets. Twin FRET efficiencies support these data, also suggesting that the two B subunits are nonadjacent in most of the heteropentamers. The high-frequency variant HTR3B p.Y129S (c.386A>C, rs11767445), linked to psychiatric disease, also forms A3B2 receptors on the plasma membrane. The 5-HT3B Y129S, subunit incorporates in a slightly (11-14%) more efficient manner than the common variant. In general, most of the subunits reside within the cell. In contrast to the findings for the plasma membrane, the relative abundances and FRET characteristics of intracellular subunits depend strongly on the transfection ratio. The straightforward and unambiguous combination of plasma membrane-sheet isolation, fluorescence intensity ratios, and FRET is a generally promising procedure for determining stoichiometry of proteins on the plasma membrane.
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