1. University of Birmingham, UK
2. University of Dundee, UK
3. University of Basel, Switzerland
4. University of Bristol, UK
5. Tufts University, USA
6. University of Ferrara, Italy
7. Emory University, USA
8. University of East Anglia, UK
9. University of Milan, Italy
10. Jerusalem College of Technology, Israel
11. Salk Institute, USA
12. Ruhr University Bochum, Germany
13. University of Illinois, USA
14. University of Copenhagen, Denmark
15. Université de Lausanne, Switzerland
16. University of Strathclyde, UK
17. University College London, UK
18. Universidad Miguel Hernández, Spain
19. University of Cambridge, UK
20. Pennsylvania State University, USA
21. University of Queensland, Australia
22. University of Colorado, USA
23. National Institutes of Health, USA
24. University of Tokyo, Japan
25. Université Bordeaux 2, France
26. Kyoto University Faculty of Medicine, Japan
27. Ludwig-Maximilians-Universität München, Germany
28. University of Heidelberg, Germany
29. University of California Los Angels, USA
30. The University of Queensland, Australia
31. Harvard Medical School, USA
32. Max Planck Institute for Medical Research, Germany
33. Medical University Vienna, Austria
34. Spedding Research Solutions SARL, France
35. University of Bath, UK

Abstract

Ligand-gated ion channels (LGICs) are integral membrane proteins that contain a pore which allows the regulated flow of selected ions across the plasma membrane. Ion flux is passive and driven by the electrochemical gradient for the permeant ions. These channels are open, or gated, by the binding of a neurotransmitter to an orthosteric site(s) that triggers a conformational change that results in the conducting state. Modulation of gating can occur by the binding of endogenous, or exogenous, modulators to allosteric sites. LGICs mediate fast synaptic transmission, on a millisecond time scale, in the nervous system and at the somatic neuromuscular junction. Such transmission involves the release of a neurotransmitter from a pre-synaptic neurone and the subsequent activation of post-synaptically located receptors that mediate a rapid, phasic, electrical signal (the excitatory, or inhibitory, post-synaptic potential). However, in addition to their traditional role in phasic neurotransmission, it is now established that some LGICs mediate a tonic form of neuronal regulation that results from the activation of extra-synaptic receptors by ambient levels of neurotransmitter. The expression of some LGICs by non-excitable cells is suggestive of additional functions.

By convention, the LGICs comprise the excitatory, cation-selective, nicotinic acetylcholine [959, 210], 5-HT₃ [68, 1441], ionotropic glutamate [856, 1375] and P2X receptors [659, 1330] and the inhibitory, anion-selective, GABA_A [1066, 83] and glycine receptors [878, 1539]. The nicotinic acetylcholine, 5-HT₃, GABA_A and glycine receptors (and an additional zinc-activated channel) are pentameric structures and are frequently referred to as the Cys-loop receptors due to the presence of a defining loop of residues formed by a disulphide bond in the extracellular domain of their constituent subunits [966, 1357]. However, the prokaryotic ancestors of these receptors contain no such loop and the term pentameric ligand-gated ion channel (pLGIC) is gaining acceptance in the literature [573]. The ionotropic glutamate and P2X receptors are tetrameric and trimeric structures, respectively. Multiple genes encode the subunits of LGICs and the majority of these receptors are heteromultimers. Such combinational diversity results, within each class of LGIC, in a wide range of receptors with differing pharmacological and biophysical properties and varying patterns of expression within the nervous system and other tissues. The LGICs thus present attractive targets for new therapeutic agents with improved discrimination between receptor isoforms and a reduced propensity for off-target effects. The development of novel, faster screening techniques for compounds acting on LGICs [359] will greatly aid in the development of such agents.

Contents

GtoPdb is an expert-driven guide to pharmacological targets and the substances that act on them. GtoPdb is a reference work which is most usefully represented as an on-line database. As in any publication this work should be appropriately cited, and the papers it cites should also be recognized. This document provides a citation for the relevant parts of the database, and also provides a reference list for the research cited by those parts. For further details see [175].

Please note that the database version for the citations given in GtoPdb are to the most recent preceding version in which the family or its subfamilies and targets were substantially changed. The links below are to the current version. If you need to consult the cited version, rather than the most recent version, please contact the GtoPdb curators.

Database links

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