TRIM25, the tripartite motif containing 25, is an E3 ubiquitin ligase. It is involved in multiple biological processes, most notably in the antiviral innate immune response by activating the RIG-I signaling pathway [3,4,5,6]. It also participates in pathways like ISGylation and has connections with the Keap1-Nrf2 pathway, playing a role in maintaining endoplasmic reticulum (ER) homeostasis [1,7].

In hepatocellular carcinoma, depletion of TRIM25 leads to ER stress and attenuates tumor cell growth both in vitro and in vivo, suggesting its importance in tumor cell survival and growth via the Keap1-Nrf2 pathway [1]. In breast cancer, its regulation and function as an E3-ligase for ubiquitin and in the ISGylation system affect the proteome of mammary tissue, being potentially a biomarker and therapeutic target [2]. In antiviral defense, it is a marker of antiviral stress granules, with its co-condensation with G3BP1 enhancing ubiquitination activity towards antiviral proteins and activating the RIG-I pathway to restrain RNA virus infection [3].

In conclusion, TRIM25 is crucial in antiviral innate immunity, cell survival, and growth, with its dysregulation associated with cancer development. Studies, including those using in vitro and in vivo models, have provided insights into its function in disease-related processes, suggesting it could be a potential target for therapies in cancer and other diseases [1,2,3].