RPN1, also known as ribophorin I, is a type I transmembrane protein that plays a vital role in glycosylation [3]. It is a part of an N-oligosaccharyl-transferase complex and has been associated with multiple biological processes and disease conditions [5].

RPN1 is involved in various cancer-related processes. Deletion of RPN1 imparts resistance to disulfidptosis, a newly discovered cell death modality. In breast and lung cancer cell lines, RPN1 primarily induces cell skeleton breakdown to facilitate disulfidptosis [1]. In hepatocellular carcinoma, the circ-SNX27/miR-375/RPN1 axis contributes to cancer progression [2]. In triple-negative breast cancer, RPN1 is aberrantly expressed, correlating with increased proliferation and poor prognosis. It mediates post-translational modification of PD-L1, enhancing its glycosylation and stability for immune escape and tumor growth, and deletion of RPN1 improves the tumor microenvironment and enhances anti-PD-1 therapy efficacy [3]. Functional validation in multiple cancer cell lines also demonstrated its role in tumor cell proliferation and migration [4]. In gliomas, RPN1 affects immune cell infiltration, prognosis, and treatment outcomes, and interference with its expression reduces glioma cell migratory and invasive ability [6]. In liver cancer, knockdown of RPN1 promoted the proliferative and invasive capacities of liver cancer cells [7].

In conclusion, RPN1 is a significant gene involved in multiple biological functions, especially in cancer-related processes. Studies on RPN1 knockout or knockdown models have revealed its role in disulfidptosis, tumor cell proliferation, invasion, immune evasion, and prognosis in various cancers, providing potential therapeutic targets for cancer treatment [1,2,3,4,6,7].