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. 2022 Nov 23;5:1283. doi: 10.1038/s42003-022-04121-1

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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. 6 — Rat VMAT2-Strep-tagII wild-type (WT) and mutants were expressed in Hek293 cells, solubilized from membranes in detergents and bound to Strep-Tactin Sepharose beads. VMAT2-Strep-tagII bound beads were transferred to 96 well filter plates and assayed for [³H]-DTBZ and [³H]-SMT binding. Bars show results from three independent experiments with either three or four replicates, Y434A was repeated twice with four replicates. [³H]-DTBZ and [³H]-SMT binding was correlated to the amount of VMAT2-Strep-tagII present in each sample, determined by SDS-PAGE and western blotting. Statistically significant differences from wild-type, as determined by one way ANOVA: Q143A, V233A-L234A, E313D, D400E-Y342H and Y434 mutants displayed differences in both [³H]-DTBZ and [³H]-SMT binding, p < 0.01. F335A-L336A abolished [³H]-DTBZ binding (p < 0.0001) and had a small but non-significant decrease in [³H]-SMT binding, while D400E abolished [³H]-SMT binding (p < 0.0001) and had a small but non-significant decrease in [³H]-DTBZ binding.