E3 ubiquitin-protein ligase TRIM38 (TRIM38)

E3 ubiquitin-protein ligase TRIM38 is a member of the tripartite motif family characterized by a RING finger, B-box domains, a coiled-coil region, and a PRY-SPRY domain[1][2]. It localizes in the cytoplasm and exhibits E3 ubiquitin ligase activity, facilitating both K48- and K63-linked ubiquitination, and also acts as a SUMO ligase[1][2]. TRIM38 modulates key innate immune pathways: it limits or promotes the stability of antiviral sensors (such as RIG-I, MDA5, cGAS, and STING) and key signaling intermediates by controlling their ubiquitination and/or sumoylation, thus regulating type I interferon responses and inflammatory cytokine production[1]. It is rapidly degraded during infection by certain viruses as a mechanism of immune evasion[1][2]. TRIM38 is critical for balancing effective antiviral immunity while preventing excessive inflammation and autoimmunity, making it a potential therapeutic target for infectious and inflammatory diseases[1]. There are currently no known drugs directly targeting TRIM38, nor clinical biomarkers established for patient selection or efficacy[1][2].

Other names

Tripartite motif-containing protein 38RING finger protein 15Zinc finger protein RoRetRNF15RORETRo/SSA ribonucleoprotein homolog

No drugs reported; mechanism of action would depend on modulation of ubiquitin or SUMO ligase activity, especially affecting protein stability and regulation of immune signaling pathways.