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. 2022 Dec 30;28:164. doi: 10.1186/s10020-022-00596-0

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© The Author(s) 2022

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/.

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Fig. 7 — A model of the regulatory mechanism of HMGB1 by USP13. USP13 regulates HMGB1 stability and nucleocytoplasmic localization via CRM1-dependent pathway. Consequently, USP13 promotes HMGB1 secretion; this axis can be inhibited by Spautin-1. E3 ligase of HMGB1 which is used for ubiquitination is not known (X). Synoviolin (SYVN1) is reported as the E3 ligase of HMGB1 using bioinformatics analysis(W Yao et al. 2021). Dotted line is hypothetical pathway in nucleus. UPS ubiquitin–proteasome system