TRIM7
Description
The TRIM7 (tripartite motif containing 7) is a protein-coding gene located on chromosome 5.
TRIM7 is an E3 ubiquitin ligase that plays a complex role in various cellular processes. It acts as both a tumor suppressor and a tumor promoter, contributing to innate immunity, regulation of ferroptosis, cell proliferation, and migration. TRIM7 exhibits antiviral activity against multiple viruses by targeting viral proteins for ubiquitination and degradation, including norovirus NTPase and SARS-CoV-2 NSP5 and NSP8. Its mechanism involves recognizing C-terminal glutamine motifs generated by viral proteases, triggering ubiquitination and degradation. TRIM7 also mediates Lys-63-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling, impacting JUN transactivation and cell proliferation. Furthermore, TRIM7 promotes TLR4-mediated signaling, leading to the production of pro-inflammatory cytokines and type I interferon. However, it negatively regulates the exogenous cytosolic DNA virus-triggered immune response by enhancing the Lys-48-linked ubiquitination of STING1, causing its degradation. TRIM7 also ubiquitinates BRMS1, a component of the SIN3-HDAC chromatin remodeling complex. In glioblastoma cells, TRIM7 modulates NCOA4-mediated ferritinophagy and ferroptosis by ubiquitinating and degrading NCOA4.
TRIM7 is also known as GNIP, RNF90.
