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. 2017 Aug 10;7:7826. doi: 10.1038/s41598-017-08453-5

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© The Author(s) 2017

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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Involvement of Thr166 of β-tubulin in cortical microtubule depolymerization. (a,b) Subcellular localization of wild type TUB4 (WT) and mutated TUB4 proteins (S95A, S115A, T166A, T166D, S314A, S314D, T366A and T366D) fused with GFP at the N-terminus. GFP-TUB4 was constitutively driven by the CaMV35S promoter in (a) (35S:GFP-TUB4) or expressed under the TUB4 own promoter in (b) (TUB4pro:GFP-TUB4). The scale bars represent 30 µm in (a) or 20 µm in (b). (c) Subcellular localization of wild type TUB4 (WT) and mutated TUB4 proteins (T166A or T166D) fused with GFP at the N-terminus (green). Cortical microtubules are visualized with mCherry-TUB6 (magenta). The scale bars represent 20 µm. (d) Profiles of fluorescence intensity of GFP and mCherry along lines shown in (c). (e) Density of microtubules labeled with the wild type TUB4 (WT) or mutated TUB4 (T166A or T166D) fused with GFP. Data are displayed as averages ± SD. The asterisk indicates significant difference from the value in wild type GFP-TUB4 (t-test, P < 0.001).