E3 ubiquitin-protein ligase TRIM48 (TRIM48)

E3 ubiquitin-protein ligase TRIM48 is a member of the tripartite motif (TRIM) protein family, characterized by a RING finger, one or two B-box domains, and a coiled-coil region[1][5][8]. TRIM48 functions as an E3 ubiquitin ligase that promotes K48-linked polyubiquitination and subsequent proteasomal degradation of specific substrates, notably protein arginine methyltransferase 1 (PRMT1)[1][3][8][9]. By targeting PRMT1, TRIM48 facilitates activation of apoptosis signal-regulating kinase 1 (ASK1), increasing oxidative stress-induced cell death, and suppresses FOXO1 transcriptional activity by preventing its methylation[3][8]. In the immune system, TRIM48 acts as a negative feedback regulator of RIG-I-mediated signaling, modulating antiviral responses and interferon production[4]. TRIM48 is implicated in cancer, immune modulation, and possibly other diseases, but no drugs are currently known to directly target it.

Other names

RNF101RING finger protein 101Tripartite motif-containing protein 48TRIM48E3 ubiquitin-protein ligase TRIM48

Targeting TRIM48 would generally modulate protein ubiquitination pathways, influencing degradation of specific targets such as PRMT1 and pathways like ASK1-mediated apoptosis and antiviral signaling