ArticleProtein expression and purification2013
Bacterially expressed human serotonin receptor 3A is functionally reconstituted in proteoliposomes.
Article in Protein expression and purification, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- A nondestructive membrane engineering method using an amphiphilic polymer.Protein science : a publication of the Protein Society · 2024Article
- Functional expression of human prostaglandin E2 receptor 4 (EP4) inBiochemistry and biophysics reports · 2021Article
- Half a Century of Research on Membrane-Containing Bacteriophages: Bringing New Concepts to Modern Virology.Viruses · 2019Review
- Determination of the endothelin-1 recognition sites of endothelin receptor type A by the directed-degeneration method.Scientific reports · 2017Article
- High yield and efficient expression and purification of the human 5-HT3A receptor.Acta pharmacologica Sinica · 2015Article
- Atomistic insights into human Cys-loop receptors by solution NMR.Biochimica et biophysica acta · 2015Article
- The oligomeric states of the purified sigma-1 receptor are stabilized by ligands.The Journal of biological chemistry · 2014Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Human serotonin receptor 3A (5-HT3A) is a ligand-gated ion channel regulated by serotonin. A fusion protein (P9-5-HT3A) of 5-HT3A with the P9 protein, a major envelope protein of bacteriophage phi6, was highly expressed in the membrane fraction of Escherichia coli, and the expressed protein was purified to homogeneity using an affinity chromatography. P9-5-HT3A was observed as mixed oligomers in detergents. The purified P9-5-HT3A was efficiently reconstituted into proteoliposomes, and the serotonin-dependent ion-channel activity of P9-5-HT3A was observed by measuring the increased fluorescence of Fluo-3 attributed to the formation of a complex with the Ca(2+) ions released from the proteoliposomes. Alanine substitution for Trp178 of 5-HT3A abolished the serotonin-dependent ion-channel activity, confirming the importance of Trp178 as a ligand-binding site. Furthermore, the ion-channel activity of the reconstituted P9-5-HT3A was effectively blocked by treatment with ondansetron, an antagonist of 5-HT3A. The bacterial expression system of human 5-HT3A and the proteoliposomes reconstituted with 5-HT3A would provide biophysical and structural analyses of 5-HT3A.
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