Tripartite motif-containing protein 8 (TRIM8)

Tripartite motif-containing protein 8 (TRIM8) is a class V member of the TRIM/RBCC family of E3 ubiquitin ligases characterized by a RING-finger domain, two B-boxes, a coiled-coil region, and a proline-rich C-terminal region. TRIM8 is involved in diverse cellular processes, including regulation of protein ubiquitination, modulation of cell proliferation, apoptosis, and the innate immune response. It exerts a dual role in oncogenesis, acting as both a tumor suppressor and an oncogene depending on cellular context (notably, through regulation of p53 and NF-κB signaling). TRIM8 plays a significant role in cytokine signaling, especially in response to TNF-α and IL-1β, and has been implicated in disease contexts such as cancer, neurodevelopmental disorders, and inflammatory diseases. No direct drugs targeting TRIM8 are currently approved or in advanced clinical use[1][2][3][4][5][6][7].

Other names

RING finger protein 27 (RNF27)Glioblastoma expressed RING-finger protein (GERP)E3 ubiquitin-protein ligase TRIM8

Promotion of substrate polyubiquitination (K6, K33, K48, K63 linkages); Modulation of signaling pathways, including enhancement or inhibition of p53, NF-κB, and STAT3 axis activity; Protein degradation via the ubiquitin-proteasome system