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. 2024 May 9;17:15. doi: 10.1186/s13072-024-00540-y

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© The Author(s) 2024

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 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. 2 — Crosstalk of UHRF1 PTMs. The impact of phosphorylation, methylation, and acetylation on UHRF1 ubiquitination or deubiquitination. These proteases affect the ubiquitination of UHRF1 through UHRF1 PTMs, affecting downstream functions of UHRF1, including inhibiting cell proliferation and migration; Promote cellular aging; Reduce methylation levels; Cancer cell resistance. The deubiquitination of UHRF1 affects its downstream functions, including inhibiting cell proliferation; Reduce binding with chromatin; Promote protein stability. Black arrows indicate the positive effects (cooperative modification crosstalk); Black perpendicular bars indicate the negative effects (antagonistic modification crosstalk)