E3 ubiquitin-protein ligase RNF125 (RNF125)

E3 ubiquitin-protein ligase RNF125 (RNF125) is an enzyme belonging to the RING finger protein family, characterized by a RING finger domain and several zinc finger motifs. It catalyzes the transfer of ubiquitin from E2 conjugating enzymes to specific substrate proteins, facilitating their proteasomal degradation. RNF125 plays a crucial regulatory role in the innate and adaptive immune response, including negative regulation of type I interferon production by targeting RIG-I, MDA5, and IPS1 for degradation, as well as promoting T-cell activation. It is also directly involved in regulating the stability of p53, JAK1, and PD-L1, linking it to tumor suppression, immune checkpoint regulation, and potentially tumor immune evasion. RNF125 dysregulation has been associated with diseases such as Tenorio syndrome, various cancers, and inflammatory disorders. RNF125 is considered a promising but currently untargeted molecule for future therapeutic interventions in oncology and immunology[1][2][4][5].

Other names

TRAC-1FLJ20456RING finger protein 125T-cell RING activation protein 1TNORSTRAC1T-cell ring protein identified in activation screen

Drugs targeting RNF125 (not established in current drug databases; in hypothetical/experimental contexts) would act by modulating its E3 ubiquitin ligase activity, thus affecting the ubiquitination and degradation of substrates such as RIG-I, MDA5, IPS1, p53, JAK1, and PD-L1[1][2][4][5]. Modulation of RNF125 could impact immune signaling or the immune checkpoint pathway by altering PD-L1 stability[5].