The impact of dysregulation SUMOylation on prostate cancer.

Abstract

Prostate cancer (PCa) remains one of the most common malignancies in men, with its development and progression being governed by complex molecular pathways. SUMOylation, a post-translational modification (PTM) that involves the covalent attachment of small ubiquitin-like modifier (SUMO) proteins to target substrates, has emerged as a critical regulator of various cellular processes such as transcription, DNA repair, cell cycle progression, and apoptosis. Emerging evidence reveals that abnormal SUMOylation may contribute to PCa pathogenesis, and notably, SUMO-associated enzymes are commonly dysregulated in PCa. This review explores the mechanisms by which SUMOylation is implicated in the regulation of key pathways, and summary aberrant expression of SUMO-related enzymes or SUMOylation sites mutations of substrtes in PCa, as well as the therapeutic implications of targeting the SUMO-related enzymes in PCa treatment.