FBXO45 enhances cell viability and glycolysis in cervical cancer via DUSP2 ubiquitination-mediated ERK1/2 activation.

F-box protein 45 (FBXO45) is implicated in tumorigenesis and progression. However, the functions and underlying mechanisms of FBXO45 in cervical cancer (CC) have not been elucidated. This study investigated the role of FBXO45 in the malignant progression of CC cells. Gene expression profiling interactive analysis, tissue microarrays, quantitative real-time PCR, and gene enrichment analysis confirmed the correlation between FBXO45 and CC. FBXO45-knockdown and FBXO45-overexpressing HeLa cells and Caski cells were utilized to evaluate cell viability, metabolic characteristics and protein expression via CCK-8, Seahorse assays, measurement of lactate production, and Western blotting (WB). A mouse xenograft model validated the effects of FBXO45 knockdown. Concurrently, FBXO45-dual specificity phosphatase 2 (DUSP2) interaction was investigated using co-immunoprecipitation and WB. Overexpression of FBXO45 in CC tissues and cell lines was observed. Functional studies revealed that FBXO45 promoted cell viability, glycolysis, and ERK1/2 activation. FBXO45 interacted with and ubiquitinated DUSP2, leading to ERK1/2 activation and enhanced glycolysis. Tissue microarrays and Spearman correlation analysis confirmed the negative correlation between FBXO45 and DUSP2 in CC tissues. In summary, our results suggest that FBXO45 enhances cell viability and glycolysis in CC via DUSP2 ubiquitination-mediated ERK1/2 activation. Our findings identify FBXO45 as a therapeutic target for CC, guiding the development of new drugs.