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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/.

PMC Copyright notice

Mapping of the TRIB1 interface associating with HNF4A. Recombinant TRIB1 or fragments thereof, harboring the indicated mutations or deletions were incubated in the presence of HNF4A-expressing HEK293T lysates. A, Interaction between TRIB1 and HNF4A does not require MEK1 or COP1 binding interface, nor is it altered by a gain-of-function mutation. B and C, Multiple TRIB1 epitopes interact with HNF4A in vitro. Bound material was isolated and analyzed by Western blot. Corresponding protein baits were imaged prior to transfer using Stain Free gels. Schema illustrates truncations employed and their relative binding to HNF4A.