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. 2017 Nov 27;7:16365. doi: 10.1038/s41598-017-16555-3

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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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FAD104 negatively regulates phosphorylation level of Smad3 with TGF-β1 treatment in HeLa cells. (A) Phosphorylation levels of Smad3 in fad104 knockdown HeLa cells. HeLa cells were transfected with siRNA targeting fad104 (sifad104-A) and treated with 1 ng/mL TGF-β1 for 6 h. (B) Phosphorylation levels of Smad3 in HeLa cells overexpressing FAD104. HeLa cells were infected with FAD104 and treated with 1 ng/mL TGF-β1 for 6 h. Whole-cell lysates were subjected to Western blot analysis and β-actin was used as a loading control. Signal intensities from phospho-Smad3, total Smad3, and β-actin were quantified using NIH-Image software. Each column represents the mean with standard deviation (n = 3). Significant differences are indicated as **p < 0.01 and *p < 0.05.