USP10 (ubiquitin specific peptidase 10) is a cytoplasmic deubiquitinating enzyme that regulates protein stability and cellular processes through removal of ubiquitin chains from target proteins. USP10 functions as a critical regulator of p53 stability by deubiquitinating p53 in the cytoplasm under normal conditions and translocating to the nucleus following DNA damage to activate p53-mediated DNA damage responses 1. The enzyme also plays essential roles in stress granule regulation and ribosome quality control by preventing G3BP1 degradation through deubiquitination, which facilitates stress granule formation and cellular stress responses 2. Additionally, USP10 promotes ribosome recycling by deubiquitinating 40S ribosomal proteins including RPS2, RPS3, and RPS10, preventing their proteasomal degradation during ribosome stalling. In cancer contexts, USP10 exhibits oncogenic functions by stabilizing proteins such as YAP/TAZ in hepatocellular carcinoma 3, KLF4 in lung cancer 4, and ANLN in esophageal squamous cell carcinoma 5. USP10 expression levels correlate with poor prognosis in multiple cancer types, suggesting its potential as a therapeutic target. The enzyme's diverse substrate specificity and cellular localization make it a key regulator of protein homeostasis, stress responses, and cancer progression.