E3 ubiquitin-protein ligase tripartite motif-containing protein 65 (TRIM65)

E3 ubiquitin-protein ligase tripartite motif-containing protein 65 (TRIM65) is a member of the TRIM protein family, defined by the presence of a RING finger domain, B-box domain, coiled-coil region, and a C-terminal SPRY domain[2][3][1]. It functions as an E3 ubiquitin ligase, selectively targeting proteins such as TNRC6 (key components of the RNA-induced silencing complex) and VCAM-1 for ubiquitination and proteasomal degradation[1][3][4]. Through these mechanisms, TRIM65 regulates post-transcriptional gene expression, modulates miRNA pathway activity, controls apoptosis and immune responses, and influences inflammation[1][2][3][4]. Elevated or reduced activity of TRIM65 has implications in pathologies including cancer, inflammatory conditions, and ischemic injury. Its precise molecular interactions and regulations remain an active area of research. No direct TRIM65-targeted drugs are currently in clinical use.

Other names

TRIM65Tripartite motif-containing protein 65E3 ubiquitin-protein ligase TRIM654732463G12Rik

Not applicable; mechanisms would theoretically involve inhibition or enhancement of TRIM65's E3 ligase activity, affecting ubiquitination of proteins such as TNRC6 or VCAM-1 if targeted[1][2][3][4].