The 5-HT₃ receptor (nomenclature as agreed by the NC-IUPHAR Subcommittee on 5-Hydroxytryptamine (serotonin) receptors [20]) is a ligand-gated ion channel of the Cys-loop family that includes the zinc-activated channels, nicotinic acetylcholine, GABA_A and strychnine-sensitive glycine receptors. The receptor exists as a pentamer of 4 transmembrane (TM) subunits that form an intrinsic cation selective channel [5]. Five human 5-HT₃ receptor subunits have been cloned and homo-oligomeric assemblies of 5-HT₃A and hetero-oligomeric assemblies of 5-HT₃A and 5-HT₃B subunits have been characterised in detail. The 5-HT₃C (HTR3C, Q8WXA8), 5-HT₃D (HTR3D, Q70Z44) and 5-HT₃E (HTR3E, A5X5Y0) subunits [26,37], like the 5-HT₃B subunit, do not form functional homomers, but are reported to assemble with the 5-HT₃A subunit to influence its functional expression rather than pharmacological profile [17,39,55]. 5-HT₃A, -C, -D, and -E subunits also interact with the chaperone RIC-3 which predominantly enhances the surface expression of homomeric 5-HT₃A receptor [55]. The co-expression of 5-HT₃A and 5-HT₃C-E subunits has been demonstrated in human colon [25]. A recombinant hetero-oligomeric 5-HT₃AB receptor has been reported to contain two copies of the 5-HT₃A subunit and three copies of the 5-HT₃B subunit in the order B-B-A-B-A [6], but this is inconsistent with recent reports which show at least one A-A interface [29,53]. The 5-HT₃B subunit imparts distinctive biophysical properties upon hetero-oligomeric 5-HT₃AB versus homo-oligomeric 5-HT₃A recombinant receptors [11,13,15,23,27,42,46], influences the potency of channel blockers, but generally has only a modest effect upon the apparent affinity of agonists, or the affinity of antagonists ([8], but see [10,12-13]) which may be explained by the orthosteric binding site residing at an interface formed between 5-HT₃A subunits [29,53]. However, 5-HT₃A and 5-HT₃AB receptors differ in their allosteric regulation by some general anaesthetic agents, small alcohols and indoles [21,44-45]. The potential diversity of 5-HT₃ receptors is increased by alternative splicing of the genes HTR3A and HTR3E [9,18,36,38-39]. In addition, the use of tissue-specific promoters driving expression from different transcriptional start sites has been reported for the HTR3A, HTR3B, HTR3D and HTR3E genes, which could result in 5-HT₃ subunits harbouring different N-termini [23,36,54]. To date, inclusion of the 5-HT₃A subunit appears imperative for 5-HT₃ receptor function.

Quantitative data in the table refer to homo-oligomeric assemblies of the human 5-HT₃A subunit, or the receptor native to human tissues. Significant changes introduced by co-expression of the 5-HT₃B subunit are indicated in parenthesis. Although not a selective antagonist, methadone displays multimodal and subunit-dependent antagonism of 5-HT₃ receptors [12]. Similarly, TMB-8, diltiazem, picrotoxin, bilobalide and ginkgolide B are not selective for 5-HT₃ receptors (e.g.[49]). The anti-malarial drugs mefloquine and quinine exert a modestly more potent block of 5-HT₃A versus 5-HT₃AB receptor-mediated responses [52]. Known better as a partial agonist of nicotinic acetylcholine α4β2 receptors, varenicline is also an agonist of the 5-HT₃A receptor [30]. Human [7,32], rat [22], mouse [31], guinea-pig [28] ferret [34] and canine [24] orthologues of the 5-HT₃A receptor subunit have been cloned that exhibit intraspecies variations in receptor pharmacology. Notably, most ligands display significantly reduced affinities at the guinea-pig 5-HT₃ receptor in comparison with other species. In addition to the agents listed in the table, native and recombinant 5-HT₃ receptors are subject to allosteric modulation by extracellular divalent cations, alcohols, several general anaesthetics and 5-hydroxy- and halide-substituted indoles (see reviews [2-3,41,50-51,56]).

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Subcommittee members: John A. Peters (Co-chairperson) Room CB 08 Carnelley Building School of Life Sciences The University of Dundee Dundee DD1 5EH Scotland UK Tim G. Hales (Co-chairperson) Center for Neuroscience Division of Medical Sciences Ninewells Hospital and Medical School The University of Dundee Dundee DD1 9SY UK Nicholas M. Barnes Neuropharmacology Research Group College of Medical and Dental Sciences University of Birmingham Edgbaston Birmingham B15 2TT UK Sarah C. R. Lummis Department of Biochemistry University of Cambridge Tennis Court Road Cambridge CB2 1QW UK Beate Niesler Institute of Human Genetics Department of Human Molecular Genetics University of Heidelberg Im Neuenheimer Feld 366 D- 69120 Heidelberg Germany