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. 2021 Nov 12;9:182. doi: 10.1186/s40478-021-01281-9

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© The Author(s) 2021

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Blocking Tyr136 phosphorylation promotes phosphorylation of αSyn at Ser129 and Tyr125 induced by CK2. WT r-αSyn or Y136A r-αSyn after 0–40 hours of incubation with CK2 and ATP was analyzed by SDS-PAGE followed by immunoblotting with a anti-pY136-αSyn antibody, b anti-pS129-αSyn antibody ab51253, and d anti-pY125-αSyn antibody. Molecular mass markers are indicated in kDa on the left side of each panel. Arrows indicate the top of the gel. Intensity ratios (%) of immunoreactive c pS129-αSyn, the sum of > 250-kDa and 16-kDa forms, and e > 250-kDa pY125-αSyn after 8 h of incubation were quantified in seven independent experiments. Data are presented as means ± standard deviation. Statistical significance was determined using the 2-tailed Student’s t test. **P < 0.01, ***P < 0.001 versus WT r-αSyn