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. 2021 Jun 10;12(6):602. doi: 10.1038/s41419-021-03857-8

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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 Co-IP analysis of 293T cells transfected with Flag-FKBP4 and the indicated plasmids, namely, HA-IKKα, HA-IKKβ, HA-IKKγ, and HA-Hsp90. FKBP4 interacted with all IKK complex subunits and Hsp90 under transfection conditions. B Co-IP analysis of endogenous FKBP4 interacting with endogenous IKKα, IKKβ, and Hsp90 in H1975 and BEAS-2B cells. C Pull down of HA-IKKβ, HA-IKKγ, and HA-Hsp90 by GST-tagged FKBP4. D Co-IP analysis of 293T cells with or without FKBP4 silencing and transfected with HA-IKKβ and Hsp90. FKBP4 knockdown impaired the interaction between Hsp90 and IKKβ under transfection conditions. E Co-IP analysis of 293T cells overexpressing or not overexpressing FKBP4 and transfected with HA-IKKβ and Hsp90. FKBP4 overexpression promoted the interaction between Hsp90 and IKKβ under transfection conditions. F Co-IP analysis showed that FKBP4 depletion blocked the interaction between Hsp90 and IKKβ in H1975 cells. G Co-IP analysis showed that FKBP4 depletion prevented the binding of IKKγ to IKKβ in H1975 cells. H Schematic illustration of FKBP4, showing the wild-type, truncation mutants (deleted PPIase or TPR domains), and point mutant (K354A) of FKBP4. I Co-IP analysis of the interaction between Hsp90/IKK and FKBP4 mutants in 293T cells transfected with the Flag-FKBP4 wild-type plasmid or plasmids harboring different mutations.