USP32 is a deubiquitinase that removes conjugated ubiquitin from target proteins, including RAB7A and LAMTOR1 1. Its primary function is to act as a positive regulator of mTORC1 signaling by mediating deubiquitination of LAMTOR1, thereby promoting the association between LAMTOR1 and the lysosomal V-ATPase complex, which subsequently activates the mTORC1 complex 1. As a cysteine-type deubiquitinase localized to the Golgi apparatus, USP32 catalyzes protein deubiquitination through its enzymatic activity and protein-binding interactions. The clinical significance of USP32 remains to be fully elucidated in the provided literature. While related deubiquitinases like USP10 regulate diverse oncogenic pathways—including p53 stability, DNA damage repair, and cancer cell proliferation across multiple tumor types—specific disease relevance and therapeutic implications for USP32 are not documented in the available abstracts. Further investigation is needed to determine whether USP32 dysfunction contributes to malignancy or other pathological conditions, and whether it represents a viable therapeutic target.