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. 2018 Jun 27;9:2504. doi: 10.1038/s41467-018-04936-9

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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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Fig. 10 — A putative working model of Smad6–PIAS3–STAT3 regulation axis. STAT3 is activated in an external stimulation-dependent manner (IL-6, EGF, or other cytokines) or external stimulation-independent manner through phosphorylation of the STAT3 tyrosine residue. Activated STAT3 forms homodimers or STAT3/STAT1 heterodimers and translocates to the nucleus to function as a transcription factor. PIAS3 binds activated STAT3 and prevents its binding to DNA, resulting in the downregulation of STAT3-dependent transcription. Undetermined signals induce Smad6 nuclear translocation. Nuclear-Smad6 indirectly activates STAT3-dependent transcription through promoting the ubiquitination