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. 2018 Mar 19;9(4):423. doi: 10.1038/s41419-018-0462-8

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© The Author(s) 2018

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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Fig. 5 — a Co-immunoprecipitation assays showed the interaction of PIWIL2, CK2α, and HDAC3. b Cell lysates were immunoprecipitated with anti-HA antibody, and then a secondary immunoprecipitation assay was performed with anti-PIWIL2 antibody. c Immunofluorescence assays showed the co-localization of PIWIL2, CK2α, and HDAC3. d, e PIWIL2 facilitates CK2α binding with HDAC3 to phosphorylate HDAC3