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Tripartite motif-containing protein 60 (TRIM60) is an E3 SUMO-protein ligase belonging to the TRIM family, notable for containing a RING finger domain involved in protein-protein and protein-DNA interactions. TRIM60 mediates SUMOylation of TAB2, resulting in the suppression of the TRAF6/TAB2/TAK1 complex and inhibition of MAPK and NF-κB signaling pathways, thereby acting as a negative regulator of proinflammatory cytokine production in macrophages and other immune cells. TRIM60 plays a critical role in the innate immune response, with deficiency leading to heightened cytokine production, increased susceptibility to septic shock, and altered responses to bacterial infection. The protein is also characterized by additional TRIM family domains, including B-box, coiled-coil, and PRY-SPRY regions involved in oligomerization and substrate selectivity. Currently, TRIM60 is not the direct target of approved drugs, but its regulatory function in immunity suggests potential relevance for future therapeutic research.
Not applicable (no known drugs)
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