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. 2018 Aug 2;38(1):17–32. doi: 10.1038/s41388-018-0414-x

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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. 3 — KDM8 regulates PKM2 nuclear translocation. a Interaction of endogenous KDM8 and PKM2 in LNCaP cells. Reciprocal immunoprecipitation (IP) and immunoblotting (IB) were performed with PKM2 and KDM8 antibodies as indicated. b Subcellular localization of KDM8 and PKM2 in LNCaP cells. Nuclear (Nuc) and cytosolic (Cyto) fractions were prepared from LNCaP cells transfected with si-NT, si-KDM8, EV, or KDM8-expressing vector, followed by immunoblotting analysis with antibodies as indicated. KDM8*, Flag-tagged KDM8. c Confocal immunomicroscopy analysis of PKM2 nuclear translocation. Treated cells were fixed and immunostained with anti-PKM2 (PKM2) and 4′,6-diamidino-2-phenylindole (DAPI, nucleus), respectively. The framed regions marked in the merged images (Merge) are zoomed at the next (Zoom). The line profiles of PKM2 and DAPI signals were measured by ZEN 2011 (Carl Zeiss, Germany) software. Scale bars, 10 µm