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. 2019 Sep 16;9:13381. doi: 10.1038/s41598-019-49821-7

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© The Author(s) 2019

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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Effect of human VRK1 pathogenic variants on chromatin substrates: histones H3, forming part of nucleosomes, and H2AX associated to the initial reaction to DNA damage. (a) Phosphorylation of histone H3 in Thr3 by different VRK1 variant proteins. The H3T3 phosphorylation was detected in immunoblots with a phosphospecific antibody. (b) Phosphorylation of histone H2AX by different VRK1 pathogenic variant proteins performed by in vitro radioactive kinase assay. The graph shows the ratio of phosphorylated and non-phosphorylated substrates for each protein. The statistical study of the variables, protein level and time is a covariance analysis by least-square non-linear regression to detect the correlation between the change in protein as a function of time. The assays were performed in triplicate and are represented individually as dots in the graph. Wild type VRK1 was the reference value. *p < 0.05, **p < 0.005, ***p < 0.0005. Western blots with the proteins used in kinase assays are shown in Supplementary Fig. S7.