MOD-1 is a serotonin-gated chloride channel that modulates locomotory behaviour in C. elegans

Rajesh Ranganathan, Stephen C. Cannon and H. Robert Horvitz ()
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Rajesh Ranganathan: Room 68-425, Massachusetts Institute of Technology
Stephen C. Cannon: Harvard Medical School, Boston, Massachusetts 02115
H. Robert Horvitz: Room 68-425, Massachusetts Institute of Technology

Nature, 2000, vol. 408, issue 6811, 470-475

Abstract: Abstract The neurotransmitter and neuromodulator serotonin (5-HT) functions by binding either to metabotropic G-protein-coupled receptors (for example, 5-HT1, 5-HT2, 5-HT4 to 5-HT7), which mediate ‘slow’ modulatory responses through numerous second messenger pathways1, or to the ionotropic 5-HT3 receptor, a non-selective cation channel that mediates ‘fast’ membrane depolarizations2. Here we report that the gene mod-1 (for modulation of locomotion defective) from the nematode Caenorhabditis elegans encodes a new type of ionotropic 5-HT receptor, a 5-HT-gated chloride channel. The predicted MOD-1 protein is similar to members of the nicotinic acetylcholine receptor family of ligand-gated ion channels, in particular to GABA (γ-aminobutyric acid)- and glycine-gated chloride channels. The MOD-1 channel has distinctive ion selectivity and pharmacological properties. The reversal potential of the MOD-1 channel is dependent on the concentration of chloride ions but not of cations. The MOD-1 channel is not blocked by calcium ions or 5-HT3a-specific antagonists but is inhibited by the metabotropic 5-HT receptor antagonists mianserin and methiothepin. mod-1 mutant animals are defective in a 5-HT-mediated experience-dependent behaviour3 and are resistant to exogenous 5-HT, confirming that MOD-1 functions as a 5-HT receptor in vivo.

Date: 2000
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DOI: 10.1038/35044083

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