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Chapter 5 : Glutamate-Activated Channels

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Glutamate-Activated Channels, Page 1 of 2

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Abstract:

Ligand-gated ion channels (LGICs) are a major class of ion channels. Postsynaptic LGICs generate electrical signals in response to specific chemical neurotransmitters such as acetylcholine, glutamate, glycine, or γ-aminobutyric acid. Understanding the polymorphism of the genes encoding the GluRs in particular will increase one's understanding of the role of these receptors in neurogenetic variations. Animal glutamate receptors possess both metabotropic glutamate receptors (mGluRs) and ionotropic glutamate receptors (iGluRs). The iGluRs and mGluRs are classified into subgroups based on their sequence homology, agonist pharmacology, and intracellular transduction mechanisms. The structural and sequence similarity of the different domains of GluRs to proteins from different types of organisms gives rise to some interesting implications in the evolutionary relationship between prokaryotes and eukaryotes. The iGluRs are classified as nmethyl-D-aspartic acid (NMDA) receptors or non-NMDA receptors, which include kainate (KAI) and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors. The first prokaryotic glutamate receptors to be discovered was GluR0 from sp. strain PCC 6803. An interesting observation was made based on scores of the similarity of profiles of the P-loop and M2 helix. Plant glutamate receptors (GLRs) were first identified in . The sequencing of the complete genome of revealed the existence of not 1 but 20 genes that encoded putative GLRs. A famous quote of Theodosius Dobzhansky, “Nothing in biology makes sense, except in the light of evolution,” emphasizes the importance of evolutionary studies in biology. Evolutionary inferences essentially rely on diversity among organisms, where the differences are accumulated randomly from some common ancestor.

Citation: Shrivastava I, Guy H. 2005. Glutamate-Activated Channels, p 83-95. In Kubalski A, Martinac B (ed), Bacterial Ion Channels and Their Eukaryotic Homologs. ASM Press, Washington, DC. doi: 10.1128/9781555816452.ch5

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Figures

Image of Figure 1.
Figure 1.

Classification of mGluRs and iGluRs based on their pharmacological activities and structural similarities.

Citation: Shrivastava I, Guy H. 2005. Glutamate-Activated Channels, p 83-95. In Kubalski A, Martinac B (ed), Bacterial Ion Channels and Their Eukaryotic Homologs. ASM Press, Washington, DC. doi: 10.1128/9781555816452.ch5
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Image of Figure 2.
Figure 2.

General structure of the membrane topology of a single subunit of mGluRs (A) and iGluRs (B).

Citation: Shrivastava I, Guy H. 2005. Glutamate-Activated Channels, p 83-95. In Kubalski A, Martinac B (ed), Bacterial Ion Channels and Their Eukaryotic Homologs. ASM Press, Washington, DC. doi: 10.1128/9781555816452.ch5
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Image of Figure 3.
Figure 3.

The predicted membrane topologies of eukaryotic GluRs, prokaryotic GluRs, and KcsA. The boxed regions indicate the ligand-binding domain (dashes) and M1-P-M2 motif (dash-dot-dash).

Citation: Shrivastava I, Guy H. 2005. Glutamate-Activated Channels, p 83-95. In Kubalski A, Martinac B (ed), Bacterial Ion Channels and Their Eukaryotic Homologs. ASM Press, Washington, DC. doi: 10.1128/9781555816452.ch5
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Image of Figure 4.
Figure 4.

Phylogenetic tree generated from parsimony analysis of amino acid sequences of rat iGluRs, GLRs, and two prokaryotic cyanobacterial iGluRs. (Reprinted from with permission.)

Citation: Shrivastava I, Guy H. 2005. Glutamate-Activated Channels, p 83-95. In Kubalski A, Martinac B (ed), Bacterial Ion Channels and Their Eukaryotic Homologs. ASM Press, Washington, DC. doi: 10.1128/9781555816452.ch5
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