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. 2019 Nov 29;9:17992. doi: 10.1038/s41598-019-54312-w

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© The Author(s) 2019

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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HDAC4 inhibits TBX5-MEF2C complex formation. (A) In vitro pulldown assay showing the interaction of TBX5 with HDAC4 and MEF2C (lanes 6 and 7)), and the interaction of MEF2C with HDAC4 and TBX5 (lanes 9 and 10). HDAC4 presents higher affinity for MEF2C than TBX5 does. Control protein luciferase (Luc) does not interact with TBX5 (lane 5) or MEF2C (lane 8). (B–D) Additional pull-down experiments indicate that increasing concentrations of HDAC4 (Fig C; lane 2 and 3) inhibit the TBX5-MEF2C complex formation. Increasing concentrations of TBX5 fail to compete out HDAC4 for MEF2C binding (Fig D; lane 2, 3 and 4).