The 5-HT3B subunit is a major determinant of serotonin-receptor function

Paul A. Davies, Marco Pistis, Michael C. Hanna, John A. Peters, Jeremy J. Lambert, Tim G. Hales and Ewen F. Kirkness ()
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Paul A. Davies: The George Washington University Medical Center
Marco Pistis: Ninewells Hospital and Medical School, The University of Dundee
Michael C. Hanna: the Institute for Genomic Research
John A. Peters: Ninewells Hospital and Medical School, The University of Dundee
Jeremy J. Lambert: Ninewells Hospital and Medical School, The University of Dundee
Tim G. Hales: The George Washington University Medical Center
Ewen F. Kirkness: the Institute for Genomic Research

Nature, 1999, vol. 397, issue 6717, 359-363

Abstract: Abstract The neurotransmitter serotonin (5-hydroxytryptamine or 5-HT) mediates rapid excitatory responses through ligand-gated channels (5-HT3 receptors). Recombinant expression of the only identified receptor subunit (5-HT3A) yields functional 5-HT3 receptors1. However, the conductance of these homomeric receptors (sub-picosiemens) is too small to be resolved directly, and contrasts with a robust channel conductance displayed by neuronal 5-HT3 receptors (9–17 pS)2,3,4,5,6,7. Neuronal 5-HT3 receptors also display a permeability to calcium ions and a current–voltage relationship that differ from those of homomeric receptors3,4,5,8. Here we describe a new class of 5-HT3-receptor subunit (5-HT3B). Transcripts of this subunit are co-expressed with the 5-HT3A subunit in the amygdala, caudate and hippocampus. Heteromeric assemblies of 5-HT3A and 5-HT3B subunits display a large single-channel conductance (16 pS), low permeability to calcium ions, and a current–voltage relationship which resembles that of characterized neuronal 5-HT3 channels. The heteromeric receptors also display distinctive pharmacological properties. Surprisingly, the M2 region of the 5-HT3B subunit lacks any of the structural features that are known to promote the conductance of related receptors. In addition to providing a new target for therapeutic agents, the 5-HT3B subunit will be a valuable resource for defining the molecular mechanisms of ion-channel function.

Date: 1999
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DOI: 10.1038/16941

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