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. 2022 Dec 21;13(12):1063. doi: 10.1038/s41419-022-05457-6

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — A Topological location of Gly-82, Leu-85, and Pro-289 residues in human EAAT2. B Comparison of the amino acid sequences of epileptic variants (G82R, L85P, and P289R) between Glt_ph and EAATs. Regions of high homology of Glt_Ph and EAATs are highlighted in blue. C D-[³H]-Asp uptake activity after transfection with different plasmids (SK, WT, G82R, L85P, P289R, G82R/L85P, G82R/P289R, L85P/P289R, and G82R/L85P/P289R) were determined. n = 6 per group. The representative blots and quantification of total proteins (D, E), biotinylated membrane proteins (F, G), and non-biotinylated proteins (H, I) of GLT-1 were measured by Western blot. n = 3 per group. Results are expressed as mean ± SD. ^**P < 0.01 vs. WT. Statistical significance was determined using one-way ANOVA and Tukey’s test for post hoc comparisons.