Ube2z, a member of ubiquitin-conjugating enzymes, is involved in FAT10 conjugation, a post-translational modification similar to ubiquitination. It functions as a conjugating (E2) enzyme along with UBA6 as the activating (E1) enzyme in this pathway. Additionally, it may also participate in ubiquitination. Ube2z is associated with multiple biological processes and has potential implications in diseases, making genetic models valuable for studying its functions [1,5].

In lung cancer, Ube2z is upregulated in lung adenocarcinoma (LUAD) tissues and cells. Knockdown of Ube2z curtails aggressive behaviors in LUAD cells, suggesting its potential as a therapeutic target [2].

In hepatocellular carcinoma (HCC), Ube2z is overexpressed, and its high expression is correlated with various clinicopathological features and poor survival. Knocking down Ube2z using siRNA can restrain tumor cell proliferation and suppress cell migration and invasion, indicating it may be a prognostic biomarker and therapeutic target for HCC [3].

BMSC-derived exosomal miR-219-5p can target Ube2z to regulate its stability, and miR-219-5p alleviates ferroptosis in neuronal cells induced by spinal cord injury through the UBE2Z/NRF2 pathway [4].

In conclusion, Ube2z plays important roles in multiple biological processes, especially in the context of cancer and ferroptosis-related pathologies. Studies, including those with knockdown models, have revealed its potential as a biomarker and therapeutic target in lung cancer and hepatocellular carcinoma, and its involvement in the miR-219-5p-mediated alleviation of ferroptosis in spinal cord injury.