E3 ubiquitin-protein ligase TRIM4 (TRIM4)

E3 ubiquitin-protein ligase TRIM4 (TRIM4) is a cytoplasmic enzyme belonging to the tripartite motif (TRIM) family of proteins, defined by its RING domain, two B-box domains, and a coiled-coil region[3]. TRIM4 acts as an E3 ubiquitin ligase, mediating the transfer of ubiquitin to specific substrate proteins, particularly influencing immune signaling pathways such as the RIG-I-dependent antiviral response through K63-linked ubiquitination of CARD domain-containing substrates[1][3]. TRIM4 has been associated with regulation of mitochondrial organization, cellular response to oxidative stress, and promotion of cell death under certain conditions[2]. Its expression is implicated in cancer biology, especially as a prognostic biomarker in hepatocellular carcinoma where decreased TRIM4 expression correlates with worse prognosis and higher recurrence risk[2]. No approved drugs directly targeting TRIM4 are currently known, and there are no specific safety concerns reported unique to its modulation.

Other names

Tripartite motif-containing protein 4RNF87RING finger protein 87RING-type E3 ubiquitin transferase TRIM4tripartite motif protein TRIM4

Ubiquitin-mediated protein degradation, Regulation of antiviral signaling via K63-linked ubiquitination, Sensitization to oxidative cell death