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. 2019 Mar 25;9:5074. doi: 10.1038/s41598-019-41640-0

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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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Protein kinase of HSP90. (A) Three protein kinases, rLmCK1.2, rDYRK 1, and rGSK 1, were incubated with γ-³²P-ATP with MBP or with HSP90wt as substrate as indicated below and analysed by SDS-PAGE and Coomassie Brilliant Blue staining. The positions of protein size markers are indicated to the left, the positions of the kinases and of HSP90 are indicated on the right. (B) As in (A), but autoradiograph. (C,D) In vitro protein kinase assay of rLmCK1.2 with HSP90 and 5 phosphosite mutants thereof, using γ-³²P-ATP. (C) shows a Coomassie Brilliant Blue stain, (D) shows the corresponding autoradiograph. (E,F) As in (C,D), but with 4 other phosphosite mutants of HSP90. (G) Mass spectrometry-based quantification of the phosphoserine/serine ratio at Ser₂₈₉ without (−D4476) or with (+D4476) a CK1.2-specific inhibitor. The y-axis is in log₁₀ scale. All greyscale images were cropped from contiguous parts of the original image. Digital enhancements, using Adobe Photoshop CS3, were performed over the entire greyscale images and restricted to tonality optimisation and size adjustments.