TRIM7, also known as RNF90, is an E3 ubiquitin ligase. It plays significant roles in various biological processes, mainly by catalyzing the ubiquitination of diverse substrates. It is involved in antiviral immunity, autophagy, ferroptosis, and tumorigenesis, making it crucial for understanding host-pathogen interactions and disease mechanisms [1-3, 8]. Genetic models, such as KO mouse models, are valuable for studying its functions.

In Trim7-/-mice infected with SARS-CoV-2, there was increased pathology, virus titers, epithelial apoptosis, and dysregulated immune responses, indicating that TRIM7 restricts viral replication and apoptosis by ubiquitinating the viral membrane protein [2,3]. In L. monocytogenes infection, TRIM7-deficient mice had elevated innate immune responses and increased infection, as TRIM7 promotes autophagosome accumulation by ubiquitinating ATG7 [1].

In conclusion, TRIM7 is essential in multiple biological processes. Its role in antiviral immunity, autophagy, and ferroptosis has been revealed through model-based research, especially KO mouse models. These findings contribute to understanding diseases like viral infections, bacterial infections, and glioblastoma, potentially guiding the development of new therapeutic strategies.