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. 2023 May 27;8:220. doi: 10.1038/s41392-023-01439-y

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© The Author(s) 2023

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. 8 — Future outlook of PTMs research. To date, there are several PTM databases, and each one contains thousands of proteins and overlapping parts. PTM crosstalk regulates multiple PTMs on the same or different protein substrates. Mass spectrometry (MS) is a commonly used tool to study PTMs, and MS-based different PTM omics indicate the potential crosstalk. Recently, the proteolysis-targeted chimerism (PROTAC) technology for targeted protein degradation is an innovative strategy to treat various diseases. PhosTAC focuses on recruiting Ser/Thr phosphatase into phosphate matrices to mediate, which can uniquely provide targeted function gain opportunities to manipulate protein activity. PhosTAC works similarly to PROTAC and has great potential as biological and pharmacological tools. The figure is generated with BioRender (https://biorender.com)