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. 2020 Jul 20;10:87. doi: 10.1186/s13578-020-00446-8

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Four regulatory mechanisms of MM-1 on c-Myc. a Rabring7 degrades c-Myc through complex formation with MM-1. b MM-1 and Egr1 cooperate in the transcriptional repression of Wnt4, which is one of the elements of the Wnt-b-catenin pathway that positively controls the c-Myc gene. c MM-1 binds the N-terminal region of c-Myc, and represses its transcriptional activity by recruiting the TIF1β co-repressor and the histone deacetylase HDAC1–mSin3 complex. d Inhibition of c-Myc activity by MM-1 can be lost due to the missense mutation of amino acid 157 from alanine to arginine (A157R)