Usp10, a ubiquitin-specific protease, is a key player in deubiquitination processes. It features the classic USP domain and is involved in regulating protein homeostasis and various cellular processes [3]. Ubiquitination and deubiquitination are important post-translational modifications that can affect protein stability, localization, and function.

Loss-of-function studies have shown significant roles of Usp10 in multiple disease-related processes. In mice, loss of Usp10 downregulates Krüppel-like factor 4 (KLF4) expression and accelerates KrasG12D-driven lung adenocarcinoma initiation and progression, indicating its role in suppressing lung tumorigenesis [2]. Depletion of Usp10 enhances polyubiquitination of Yes-associated protein (YAP)/transcriptional coactivator with PDZ-binding motif (TAZ), promotes their proteasomal degradation, and arrests the proliferation of hepatocellular carcinoma both in vitro and in vivo [1].

In conclusion, Usp10 is a crucial regulator in multiple biological processes, especially in cancer-related pathways. Through gene knockout or conditional knockout mouse models, it has been revealed that Usp10 can act as a suppressor in lung cancer and may play a role in regulating the progression of hepatocellular carcinoma, providing potential therapeutic targets for these diseases.