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Abstract
The ubiquitin–proteasome system enables post-transcriptional protein modification and is a major pathway for the degradation of most of them in eukaryotic cells. Among these, the ubiquitin-specific protease (USP) family is the most extensively studied. As an important member of the USP family, ubiquitin-specific protease 39 (USP39) plays an essential role in RNA splicing and protein regulation. This review comprehensively summarizes the structural characteristics and molecular functions of USP39, emphasizing its pivotal role in the regulation of cellular processes. Dysregulation of USP39 is closely associated with the progression of various cancers through mechanisms such as immune evasion, modulation of oncogenic signaling pathways, and altered RNA splicing. These processes impact key aspects of cancer biology, including proliferation, metastasis, and therapy resistance, underscoring the broad implications of USP39 in tumor progression. Recent studies position USP39 as a promising target for cancer treatment. Future research should explore its upstream regulatory networks, develop small-molecule inhibitors, and evaluate its potential for precision oncology. This review integrates the latest insight into USP39, providing a foundation for its clinical application in cancer therapy.