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. 2020 Apr 22;10:115. doi: 10.1038/s41398-020-0797-7

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© The Author(s) 2020

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. 1 — a Setdb1 gene structure containing a Tudor domain, encoding protein MBD binding domain. The SET domain contains a ubiquitination (Ub) site on lysine-867. b SETDB1/KAP1/KRAB-Zfp complex. SETDB1 interacts with KAP1 and is recruited by KRAB-Zfp in a sequence-specific manner. The H3K9me3 signal is established and recognized by HP-1; together with other repressive signals from the SIN3A/HDAC1/2 corepressor complex and the Mi-2/NuRD (nucleosome remodeling deacetylase) local transcriptional repression is established. c SETDB1/MBD-1/ATF7IP complex mediates the interaction between H3K9me3 and DNA methylation. DNA methyltransferases (DNMTs) also interacts with SETDB1.