TRIM45 is an E3 ubiquitin ligase that plays diverse roles in cellular regulation, inflammation, and cancer biology. As a member of the tripartite motif (TRIM) family, TRIM45 contains a RING finger domain that confers E3 ubiquitin ligase activity and exhibits both cytoplasmic and nuclear localization 1. The protein functions as a transcriptional repressor in mitogen-activated protein kinase signaling pathways, inhibiting transcriptional activities of ELK-1 and AP-1 1. TRIM45 demonstrates context-dependent roles in different pathological conditions. In inflammatory responses, it aggravates microglia pyroptosis in septic encephalopathy through the Atg5/NLRP3 axis, promoting neuroinflammation 2. The protein also restricts influenza virus infection by promoting chaperone-mediated autophagic degradation of viral PB2 protein through K48-linked polyubiquitination of calpain 1 3. In cancer biology, TRIM45 exhibits tumor suppressor functions in glioma by stabilizing p53 through K63-linked ubiquitination, preventing its degradation 4. Similarly, it suppresses non-small cell lung cancer development by inducing G1 arrest and promoting apoptosis via p38 activation and ERK inhibition 5. However, TRIM45 can also promote hepatocellular carcinoma progression by facilitating fatty acid synthesis through FABP5 ubiquitination and nuclear translocation 6.