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. 2023 Apr 20;14:2174. doi: 10.1038/s41467-023-37815-z

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© The Author(s) 2023

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. 5 — a Expression of α-synuclein (α-syn) and β-actin in the SH-SY5Y cells stably expressing α-synuclein. Typical Western blot images in three independent experiments are shown. b Effects of bafilomycin A1 (BFA; 5 nM), SCH28080 (SCH; 10 μM), and vonoprazan (Vono; 10 μM) on the phosphorylated α-synuclein (α-syn) level in the cells stably expressing α-synuclein. Scale bars, 10 µm. The size of phosphorylated α-synuclein accumulation was measured. (n = 40 cells in three independent experiments). Statistical significance was determined by two-tailed unpaired Student’s t test. c Typical microscopic images of differentiated and undifferentiated (control) SH-SY5Y cells in three independent experiments. The control cells were differentiated by treatment with 10 μM retinoic acid for 3 days and 50 ng/ml of BDNF for another 3 days. Scale bars, 10 µm. d Effects of bafilomycin A1 (BFA; 5 nM), SCH28080 (SCH; 10 μM), and vonoprazan (Vono; 10 μM) on the phosphorylated α-synuclein (α-syn) level in the differentiated SH-SY5Y cells. Scale bars, 10 µm. The size of phosphorylated α-synuclein accumulation was measured. (n = 40 cells in three independent experiments). Statistical significance was determined by two-tailed unpaired Student’s t test. e Schematic model showing the property of ATP13A2 in the lysosome. ATP13A2 (A2) functions as an H⁺,K⁺-ATPase, and its inhibition by P-CABs leads to lysosomal alkalinization and α-synuclein accumulation. V, vacuolar H⁺-ATPase. PA, polyamines. All data are presented as mean ± SD. Source data are provided as a source data file.