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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 VRK1 pathogenic variants on the phosphorylation of 53BP1implicated in DNA repair by NHEJ, and phosphorylation of coilin implicated in the assembly of Cajal bodies. (a) VRK1 autophosphorylation and phosphorylation of 53BP1. As substrate, a construct of GST fused to the N-terminal domain of 53BP1 (1–346) was used. The phosphorylation was performed in an in vitro kinase assay. (b) VRK1 autophosphorylation and phosphorylation of coilin. As substrate, a construct of GST fused to the coilin domain (160–264) was used. The in vitro kinase assay was performed with radiolabeled ATP. The graph shows the ratio of phosphorylated and non-phosphorylated substrates. The statistical analysis is two-sided t-test with Welch’ correction. 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.