E3 ubiquitin-protein ligase TRIM15 (TRIM15)

E3 ubiquitin-protein ligase TRIM15 is a cytoplasmic enzyme belonging to the tripartite motif (TRIM) family, characterized by three zinc-binding domains (RING finger, B-box type 1, B-box type 2) and a coiled-coil region[1][2][3]. TRIM15 acts as an E3 ubiquitin ligase, regulating the ubiquitin-proteasome pathway to control protein degradation. It promotes cell proliferation and metastasis in various cancers by targeting substrates such as Keap1 for proteasomal degradation, thereby modulating key cellular pathways including the Nrf2 antioxidant pathway and ERK1/2 signaling[2][3][5]. TRIM15 also functions in innate immunity, contributing to interferon induction and viral defense by modulating pathways like RIG-I-MAVS and interacting with focal adhesion components to regulate cell migration and chemotaxis[3][6][7]. Its dysregulation has been linked to oncogenesis, making it a potential therapeutic target, especially in lung, melanoma, and pancreatic cancers[2][5].

Other names

Tripartite motif-containing protein 15RNF93ZNF178ZNFB7RING finger protein 93Zinc finger protein 178Zinc finger protein B7

Ubiquitination and proteasomal degradation of substrate proteins; activation of MAPK/ERK pathway; degradation of Keap1 to activate Nrf2 pathway