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. 2021 Aug 23;11:17069. doi: 10.1038/s41598-021-96627-7

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Pseudoacetylation of KXGS motif impairs MT binding. (A,B) A cell-based MT binding assay performed on lysate from HEK293T cells transfected with 0N4R WT tau or (C–F) 0N4R tau acetylation mimetics. Without Paclitaxel, most of the tubulin is unpolymerized and in the soluble fraction (A). With Paclitaxel, tubulin monomers polymerize as MTs in the pellet fraction (B). In the presence of Paclitaxel, tau acetylation mimetics (C) K259Q, (D) K290Q, (E) K321Q, and (F) K353Q lead to significant impairment of MT binding compared to WT tau. Immunoblots with antibody specific for β-tubulin (clone TUB 2.1) used to track tubulin polymerization or 3026 antibody specific for total tau. S supernatants; P pellet fractions. The relative molecular weight markers are shown on the left. (G) One-way ANOVA with Dunnett’s test was performed with N = 3 for each group. ****p < 0.0001.