USP31 confers radio-resistance in cervical cancer cells via ferroptosis pathway by deubiquitinating and stabilizing GPX4
Ubiquitin-specific peptidase 31 (USP31), a member of the deubiquitinating enzyme family, linked to the pathogenesis of cervical cancer (CC). Despite this association, the precise mechanisms underlying its role remain inadequately understood. Recent studies have identified ferroptosis as a potential mechanism contributing to radiotherapy-mediated tumor suppression and the development of radioresistance. Consequently, this research seeks to inspect the regulatory effect of USP31 in the radioresistance of CC cells, with particular emphasis on the ferroptosis pathway. Our findings indicate that USP31 levels increase in human CC cells after radiation exposure. The knockdown of USP31 through transfection with si-USP31 significantly enhanced the radiosensitivity of SiHa and HeLa cells. This knockdown also promoted ferroptosis, as evidenced by enhanced lipid reactive oxygen species (ROS) generation, higher endocellular Fe