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. 2017 Jul 17;7:5574. doi: 10.1038/s41598-017-05768-1

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© The Author(s) 2017

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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A CEBPA derived peptide interferes with CEBPA binding, but not HNF4A binding, to GST-TRIB1. Pull-down assays of CEBPA-HA and HNF4A. A, lysates of HEK293T transfected with plasmids coding for CEBPA-HA were incubated with GST-TRIB1 or GST in the presence of increasing concentrations of either a peptide matching the CEBPA interface (CEBPAp) or a control (Ctlp), substituted peptide. CEBPA in isolates was quantified by Western blotting and protein input by Ponceau. B, as in A except that lysates expressing either HNF4A or CEBPA were used in each pull-down assay. Where indicated, 10 µg of either peptide were used. Experiments were performed twice with comparable results.