TRIM47, a member of the tripartite motif-containing protein family, functions as an E3 ubiquitin ligase. It is involved in multiple biological processes and signaling pathways, such as the NF-κB, MAPK, and STAT3 signaling pathways, and plays a significant role in various diseases [1,3,4,5,6,7,8]. Genetic models, like knockout (KO) or conditional knockout (CKO) mouse models, are valuable for studying its functions.

In LPS-induced acute lung injury in mice, TRIM47-deficient mice were resistant to the injury and death, with attenuated pulmonary inflammation. TRIM47 promoted the K63-linked ubiquitination of TRAF2, activating NF-κB and MAPK signaling pathways in endothelial cells [1]. In hepatocellular carcinoma, TRIM47 knockdown led to HCC ferroptosis induction, mainly through CDO1-mediated regulation of GSH synthesis [2]. In gastric cancer, knockdown of TRIM47 inhibited cell proliferation, migration, and invasion, while overexpression promoted these behaviors, and TRIM47 was found to interact with CYLD protein, promoting its K48-linked ubiquitination and degradation [4]. In prostate cancer, TRIM47 knockdown inhibited cell proliferation, cell cycle, migration, and invasion, and promoted apoptosis, and TRIM47 was shown to bind to MDM2 and regulate MDM2/p53 expression [7]. In ovarian cancer, TRIM47 knockdown suppressed cell proliferation, invasion, migration, and epithelial-mesenchymal transition, and inhibited tumor growth in xenograft assays, by suppressing STAT3 phosphorylation [8].

In conclusion, TRIM47 is an E3 ubiquitin ligase that significantly impacts disease-related biological processes. Model-based research, especially using KO/CKO mouse models, has revealed its role in diseases like acute lung injury, hepatocellular carcinoma, gastric cancer, prostate cancer, and ovarian cancer. These findings enhance our understanding of disease mechanisms and suggest TRIM47 as a potential therapeutic target.