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. 2019 Nov 29;9:17992. doi: 10.1038/s41598-019-54312-w

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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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PRKD1 relieves HDAC4 and 5-mediated repression of TBX5. (A) Luciferase-reporter assay showing that CaMKII and CaMKIV can not relieve HDAC4/5-mediated repression of TBX5 on a MYH6 promoter fragment. (B) Luciferase-reporter assay shows that PRKD1 does relieve the HDAC4 and HDAC5-mediated repression of TBX5 on the MYH6 promoter. Results are means from three individual experiments, error bars represent SD, *p < 0.05. (C) Western blot showing the level of PRKD1, CaMKII and CaMKIV proteins used for phosphorylation assays. Full-length blot is shown Supplementary Fig. S4. (D) In vitro phosphorylation activity of PRKD1, CaMKII and CaMKIV on HDAC5 phosphorylation motifs MT1 (S259) and MT2 (S498) (bottom arrowhead). Both motifs were strongly phosphorylated by PRKD1, whereas phosphorylation by CaMKII/CaMKIV was very much weaker.