E3 ubiquitin-protein ligase TRIM52 (TRIM52)

E3 ubiquitin-protein ligase TRIM52 is a member of the tripartite motif (TRIM) family of proteins, characterized by a RING domain that confers E3 ligase activity, and unique sequence features distinguishing it from other TRIM family members[1][2]. TRIM52 participates in the ubiquitin-proteasome system, targeting specific proteins—including itself—for degradation; it is unusually unstable and tightly regulated by multiple giant E3 ligases (such as BIRC6, HUWE1, and UBR4/KCMF1)[1][4]. TRIM52 maintains genomic DNA integrity by limiting the accumulation of topoisomerase 2 DNA adducts and acts to prevent cell cycle arrest via the p53 pathway—loss of TRIM52 results in increased DNA lesions, p53 activation, and decreased cell fitness[1]. It is upregulated in various cancers, where it contributes to cell proliferation and survival in a context-dependent manner[1][3]. In addition to its role in cell division and DNA repair, TRIM52 can act as an antiviral factor, such as inhibiting Japanese Encephalitis Virus replication by targeting viral proteins for degradation via the ubiquitin-proteasome system[2]. Its functions are essential in some cancer cell backgrounds and may represent a potential, although as-yet untargeted, therapeutic vulnerability[3].

Other names

RING finger protein 102RNF102Tripartite motif-containing protein 52

Ubiquitination and proteasomal degradation of substrate proteins; mechanism for drugs would be inhibition or modulation of E3 ligase activity, but no drugs currently reported