Mol Cell Neurosci 2006 Dec 01;334:358-70. doi: 10.1016/j.mcn.2006.08.004.

Investigation via ion pore transplantation of the putative relationship between glutamate receptors and K+ channels.

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The pore domains of ionotropic glutamate receptors (iGluRs) and potassium channels (K(+) channels) show several structural similarities. To test for functional compatibility, we transferred pore regions from prokaryotic, invertebrate, and vertebrate K(+) channels into pharmacologically representative iGluRs and vice versa. Although the chimeric proteins were expressed on the cell surface, only one of 45 pore chimeras showed ion channel function: The kainate receptor subunit GluR6, carrying the pore loop plus adjacent transmembrane domains of the prokaryotic, glutamate-gated, K(+)-selective GluR0, adopted several electrophysiological properties of the donor pore upon pore transplantation. This suggests that, despite structural similarities between iGluR and K(+) channel pores, there is a lack of functional compatibility so that K(+) channel pores cannot be gated by the iGluR gating machinery, and vice versa. However, K(+)-selective pores can be gated in an iGluR sequence environment, given a similar signal transduction mechanism as appears to be present in GluR0.

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Species referenced: Xenopus
Genes referenced: grik2