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Molecular basis for convergent evolution of glutamate recognition by pentameric ligand-gated ion channels.

Lynagh, Timothy and Beech, Robin N. and Lalande, Maryline J. and Keller, Kevin and Cromer, Brett A. and Wolstenholme, Adrian J. and Laube, Bodo (2015):
Molecular basis for convergent evolution of glutamate recognition by pentameric ligand-gated ion channels.
In: Scientific reports, p. 8558, 24, (5), ISSN 2045-2322, [Article]

Abstract

Glutamate is an indispensable neurotransmitter, triggering postsynaptic signals upon recognition by postsynaptic receptors. We questioned the phylogenetic position and the molecular details of when and where glutamate recognition arose in the glutamate-gated chloride channels. Experiments revealed that glutamate recognition requires an arginine residue in the base of the binding site, which originated at least three distinct times according to phylogenetic analysis. Most remarkably, the arginine emerged on the principal face of the binding site in the Lophotrochozoan lineage, but 65 amino acids upstream, on the complementary face, in the Ecdysozoan lineage. This combined experimental and computational approach throws new light on the evolution of synaptic signalling.

Item Type: Article
Erschienen: 2015
Creators: Lynagh, Timothy and Beech, Robin N. and Lalande, Maryline J. and Keller, Kevin and Cromer, Brett A. and Wolstenholme, Adrian J. and Laube, Bodo
Title: Molecular basis for convergent evolution of glutamate recognition by pentameric ligand-gated ion channels.
Language: English
Abstract:

Glutamate is an indispensable neurotransmitter, triggering postsynaptic signals upon recognition by postsynaptic receptors. We questioned the phylogenetic position and the molecular details of when and where glutamate recognition arose in the glutamate-gated chloride channels. Experiments revealed that glutamate recognition requires an arginine residue in the base of the binding site, which originated at least three distinct times according to phylogenetic analysis. Most remarkably, the arginine emerged on the principal face of the binding site in the Lophotrochozoan lineage, but 65 amino acids upstream, on the complementary face, in the Ecdysozoan lineage. This combined experimental and computational approach throws new light on the evolution of synaptic signalling.

Journal or Publication Title: Scientific reports
Volume: 24
Number: 5
Divisions: 10 Department of Biology
10 Department of Biology > Neurophysiology and Neurosensory Systems
Date Deposited: 03 Mar 2015 10:19
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