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. 2021 Jun 2;4:663. doi: 10.1038/s42003-021-02187-x

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© The Author(s) 2021

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 IKKε v2 presents higher phosphorylation status. HEK293 cells were transfected with each Flag-IKKε isoform accompanied with or without HA-ubi. Immunoprecipitation was performed with anti-Flag beads and the resulting products were detected by anti-phospho-Serine (pSer) and anti-Flag antibodies. b, c K63R ubiquitin markedly reduces IKKε v2 phosphorylation. HEK293 cells were transfected with each Flag-IKKε isoform accompanied with wild-type or K63R HA-ubi. Immunoprecipitation was performed with anti-Flag beads and the resulting products were further assayed by immunoblot with anti-phospho-Serine, anti-Flag, and anti-HA antibodies (b) and in vitro kinase assay (c). β-actin was served as an internal control. d Molecular mechanism of IKKε isoform switching in EV71 infection.