Abstract: Non-small cell lung cancer (NSCLC), as the main histological subtype of lung cancer, has consistently ranked among the top malignant tumors in terms of incidence and mortality worldwide. With the advancement of high-throughput sequencing and proteomics technologies, the regulatory roles of deubiquitinating enzymes (DUBs) family members in the pathological process of NSCLC have increasingly attracted attention. Notably, ubiquitin-specific peptidase 32 (USP32) possesses unique substrate recognition properties and multi-dimensional regulatory functions. It deeply participates in the pathological processes of malignant transformation, proliferation, invasion, and distant metastasis of NSCLC by coordinating the stability of key oncogenic proteins, maintaining genomic integrity, and remodeling the tumor microenvironment and other molecular pathways. This review systematically analyzes the molecular interaction network of USP32 in the occurrence and development of NSCLC, with a focus on clarifying its molecular mechanism of regulating tumor signal transduction through the ubiquitin-proteasome system, providing theoretical support for the development of innovative molecular targets and precise diagnosis and treatment strategies based on DUBs regulation.