E3 ubiquitin-protein ligase TRIM56 (TRIM56)

E3 ubiquitin-protein ligase TRIM56 (TRIM56) is a member of the tripartite motif (TRIM) family and contains a RING domain, B-box domains, a coiled-coil region, and a C-terminal segment essential for its function[1][3][4][5]. TRIM56 acts primarily as an E3 ubiquitin ligase, facilitating the transfer of ubiquitin from E2 enzymes to substrate proteins, thereby regulating their stability, signaling, or localization—a process important for innate immunity, antiviral defense, and cellular homeostasis[1][3][4]. It mediates the K63-linked ubiquitination of STING and monoubiquitinates cGAS, amplifying production of type I interferons and antiviral cytokines in response to dsDNA viruses[1][4]. TRIM56 restricts replication of bovine viral diarrhea virus, dengue virus, yellow fever virus, and porcine epidemic diarrhea virus in an E3 ligase-dependent manner[1][2][5]. In cancer, TRIM56 has dual roles, suppressing ovarian cancer by promoting vimentin degradation, but supporting breast cancer cell proliferation by stabilizing estrogen receptor α[1]. Its gene is inducible by interferon and virus, and its protein expression is regulated by both transcriptional and post-translational events[2][4][5]. Structural studies indicate that TRIM56 assembles into an antiparallel tetramer via its coiled-coil domain, creating a scaffold that facilitates substrate recruitment and ubiquitin transfer activity[1][3].

Other names

Tripartite motif-containing protein 56RING finger protein 109RNF109RING-type E3 ubiquitin transferase TRIM56

Not applicable due to lack of direct drug interactions; TRIM56 itself mediates ubiquitination of select proteins involved in antiviral and cellular signaling pathways.