USP3: Key deubiquitylation enzyme in human diseases.

Ubiquitination and deubiquitylation are pivotal posttranslational modifications essential for regulating cellular protein homeostasis and are implicated in the development of human diseases. Ubiquitin‐specific protease 3 (USP3), a member of the ubiquitin‐specific protease family, serves as a key deubiquitylation enzyme, playing a critical role in diverse cellular processes including the DNA damage response, cell cycle regulation, carcinogenesis, tumor cell proliferation, migration, and invasion. Despite notable research efforts, our current understanding of the intricate and context‐dependent regulatory networks governing USP3 remains incomplete. This review aims to comprehensively synthesize existing published works on USP3, elucidating its multifaceted roles, functions, and regulatory mechanisms, while offering insights for future investigations. By delving into the complexities of USP3, this review strives to provide a foundation for a more nuanced understanding of its specific roles in various cellular processes. Furthermore, the exploration of USP3's regulatory networks may uncover novel therapeutic strategies targeting this enzyme in diverse human diseases, thereby holding promising clinical implications. Overall, an in‐depth comprehension of USP3's functions and regulatory pathways is crucial for advancing our knowledge and developing targeted therapeutic approaches for human diseases. This review aims to highlight the function of ubiquitin‐specific protease 3 (USP3) in human disease. First, we show that USP3 is crucial in maintain genomic integrity and DNA damage response. Second, we identify USP3 as a potential promising therapeutic target to overcome chemotherapy or radiotherapy resistance. Third, the significant functions of USP3 in human cancers render it a potential therapeutic and prognostic biomarker of cancers. Finally, we consider the future of USP3 research. [ABSTRACT FROM AUTHOR]