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. 2023 Jan 13;14:201. doi: 10.1038/s41467-023-35795-8

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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. 4 — a HIF-1α is regulated by acetyl-inactivated degron, hydroxyl-activated degron, and methyl-activated degron. p300 acetyltransferase generates acetyl-inactivated degron of HIF-1α and HIF-1α acetylation triggers stabilization in acetylation-dependent manner. Because hydroxylation stimulates methyl-activated degron of HIF-1α, hydroxylation reduces protein stability of HIF-1α directly or indirectly. b Examples of the regulation of protein stability by SUMOylation. SUMOylation of PML-RAR induces poly-ubiquitination and further degradation of PML-RAR. In contrast, SUMOylation and multiple phosphorylations of tau cooperatively increase protein stability of Tau.