USP24 (ubiquitin specific peptidase 24) is a deubiquitinating enzyme that regulates protein stability by removing ubiquitin modifications from target proteins. The enzyme demonstrates context-dependent functions across different cellular processes and disease states. In cancer contexts, USP24 exhibits dual roles: it promotes tumorigenesis in hepatocellular carcinoma by stabilizing TRAF2 and activating AKT/NF-κB signaling 1, while also promoting autophagy-dependent ferroptosis by reducing K48-linked ubiquitination of Beclin1 2. In gastric cancer, USP24 accelerates glycolysis and tumor progression through PLK1 stabilization and NOTCH1 activation 3. The enzyme plays a critical role in immune regulation by stabilizing PD-1 in CD8+ T cells, with IL-6/STAT3 transcriptionally activating USP24 expression, leading to T cell exhaustion and immunotherapy resistance 4. In metabolic disease, USP24 promotes lipogenesis and inflammation by stabilizing PKA-Cα 5. In Parkinson's disease, elevated USP24 levels negatively regulate autophagy by affecting ULK1 stability 6. USP24 expression is transcriptionally regulated by NF-κB 7. Therapeutically, USP24 inhibitors show promise in overcoming drug resistance by activating autophagy and maintaining genomic stability 8.