A brief overview of the E3 ubiquitin ligase: TRIM7.

TRIM7, a member of the E3 ubiquitin ligase family, has garnered significant attentions in different research fields since its discovery. This enzyme plays indispensable roles in various pathophysiological processes through ubiquitination-mediated degradation of diverse protein substrates. This review systematically summarizes the current knowledge on the protein structure and biological functions of TRIM7. Structurally, TRIM7 features a conserved RBCC motif (RING, B-box, and coiled-coil domains) coupled with a variable C-terminal region that dictates the substrate specificity. In infectious contexts, TRIM7 is required for the pathogen-specific regulation, and exerts paradoxical effects by either promoting host defense or facilitating viral pathogenesis depending on pathogen type. Within oncology, TRIM7 manifests tumor-suppressive properties through regulating metastasis, apoptosis, and tumor immunology. In addition, it might serve as a reliable biomarker for monitoring the progression of idiopathic pulmonary fibrosis and also inhibits the progression of atherosclerosis. In summary, TRIM7 plays critical roles in different pathophysiological processes, and it might be a predictive and therapeutic target in certain human diseases.