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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. 4 — a, b IRF7 preferentially interacts with IKKε v2 in the presence of ubiquitin. IRF7 and each IKKε isoform were ectopically expressed in HEK293 cells in the presence of ubiquitin. The lysates were subjected to immunoprecipitation to precipitate Flag-IKKε (a) or Flag-IRF7 (b) with anti-Flag beads, respectively. V5-IRF7 (a) and V5-IKKε isoforms (b) were detected by anti-V5 antibody. c IKKε v2 strongly interacts with endogenous IRF7 in presence of ubiquitin. RD cells were cotransfected with each Flag-IKKε isoform and HA-ubi. Total lysates were adapted to immunoprecipitation using anti-Flag beads and endogenous IRF7 was detected by anti-IRF7 antibody. β-actin was served as an internal control.