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. 2018 Aug 24;8:12780. doi: 10.1038/s41598-018-29448-w

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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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PIASγ interacts with HNF-1A. (a) Co-immunoprecipitation analysis of HNF-1A and PIASγ from HEK293 cells transiently transfected with V5-tagged HNF-1A or empty vector together with Flag-tagged PIASγ. Cells were lysed and subjected to immunoprecipitation using anti-V5 antibody. The precipitates (left) and 10 µg input (right) were separated by SDS-PAGE and immunoblotting using anti-Flag and anti-V5 antibodies. This experiment was replicated in two independent experimental days (n = 2). (b) Mutation of K205, K273 and K506 in HNF-1A does not affect the binding of PIASγ to HNF-1A. HEK293 cells were transiently transfected with WT HNF1A, K205R, K273R or K506R, together with Flag-tagged PIASγ. Lysates were analyzed similarly as described in (a) using anti-V5 antibody immunoprecipitation, SDS-PAGE analysis and immunoblotting. Full-length blots are presented in Supplementary Fig. S8. This experiment was replicated in two independent experimental days (n = 2).