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Communications Biology

Communications Biology

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USP24 promotes autophagy-dependent ferroptosis in hepatocellular carcinoma by reducing the K48-linked ubiquitination of Beclin1

Published:8 October 2024 DOI: 10.1038/s42003-024-06999-5 PMID: 39379617
Jiahui Cao, Shitao Wu, Senfeng Zhao, Libo Wang, Yahui Wu, Liming Song, Chenguang Sun, Yin Liu, Zhipu Liu, Rongtao Zhu, Ruopeng Liang, Weijie Wang, Yuling Sun

Abstract

Ubiquitination is a post-translational modification (PTM), which is critical to maintain cell homeostasis. Ubiquitin-specific protease 24 (USP24) plays roles in various diseases, the mechanisms by which USP24 regulates hepatocellular carcinoma (HCC) remain poorly understood. In this study, USP24 is found to be significantly downregulated in HCC. Knocking down USP24 promotes HCC proliferation and migration, whereas USP24 overexpression inhibits HCC in vitro and in vivo. The endogenous interaction between USP24 and Beclin1 is confirmed. Mechanically, USP24 delays Beclin1 degradation by reducing its K48-linked ubiquitination, the effects of overexpressing USP24 on HCC proliferation can be partially reversed by silencing Beclin1. We find that increased autophagy is accompanied by ferroptosis in USP24 overexpressed HCC cells and USP24 increases the susceptibility of HCC to sorafenib. Collectively, this study highlights the critical role of USP24 in regulating autophagy-dependent ferroptosis by decreasing Beclin1 ubiquitination, suggesting that targeting USP24 may be a strategy for treating HCC. The deubiquitinase USP24 stabilizes Beclin1 by decreasing its K48-linked ubiquitination. The interaction between USP24 and Beclin1 represents a key molecular mechanism that promotes autophagy related ferroptosis in HCC.

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