KAT3B acts as an oncogene in PCa by mediating the succinylation of c-Myc and promoting its stability

As a form of protein modification, succinylation significantly impacts protein function and helps govern a range of signaling mechanisms. This study was designed to explore the role of KAT3B, functioning as a succinylase, in the context of prostate cancer (PCa).

The expression levels were assessed using quantitative real-time PCR, Western blot, and immunofluorescence staining. To investigate protein-protein interactions, immunoprecipitation assays were performed. The interaction between proteins were confirmed by Co-immunoprecipitation assay. The cell phenotype of PCa cells was analyzed by CCK-8, flow cytometry, and transwell assays.

We found that KAT3B was over-expressed in PCa tumor tissues and cells. Downregulated KAT3B decreased the viability, migration, and invasion while accelerating the apoptosis of PCa cells. Mechanistically, KAT3B mediated the succinylation of c-Myc, meantime promoted the stability of c-Myc. c-Myc overexpression reversed the role of KAT3B in PCa cells. The in vivo study verified that KAT3B silencing inhibited the growth of PCa cancer tissues.

Our research indicates that KAT3B was highly expressed in PCa. KAT3B silencing inhibited PCa cell growth and cancer tissues growth by decreasing the succinylation and expression of c-Myc. These findings potentially contribute to novel approaches in diagnosing and treating PCa.