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

Timothy Lynagh; Robin N. Beech; Maryline J. Lalande; Kevin Keller; Brett A. Cromer; Adrian J. Wolstenholme; Bodo Laube

doi:10.1038/srep08558

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

Timothy Lynagh^*, Robin N. Beech, Maryline J. Lalande, Kevin Keller, Brett A. Cromer, Adrian J. Wolstenholme, Bodo Laube

^*Corresponding author for this work

16 Citations (Scopus)

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.

Original language	English
Article number	8558
Journal	Scientific Reports
Volume	5
ISSN	2045-2322
DOIs	https://doi.org/10.1038/srep08558
Publication status	Published - 1 Jan 2015

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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.",

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AU - Cromer, Brett A.

AU - Wolstenholme, Adrian J.

AU - Laube, Bodo

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AB - 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.

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

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