Tripartite motif-containing protein 43 (TRIM43)

Tripartite motif-containing protein 43 (TRIM43) is a member of the TRIM family of E3 ubiquitin ligases, characterized by N-terminal RING, B-box, and coiled-coil domains. It localizes predominantly to the cytoplasm and the centrosome. TRIM43 regulates the structural integrity of the centrosome and nuclear lamina by mediating the ubiquitination and proteasomal degradation of pericentrin during herpesvirus infections. This activity restricts herpesviral replication by altering the nuclear environment required for viral chromatin transcription, positioning TRIM43 as a host restriction factor with roles in intrinsic antiviral immunity. It is implicated in the pathogenesis of herpesvirus infections and is associated with regulating gene expression via its effects on nuclear architecture. Mutations or dysregulation in TRIM43 are linked to diseases such as facioscapulohumeral muscular dystrophy and possibly cancer[1][2][3][6][7][10].

Other names

TRIM43Atripartite motif containing 43

Ubiquitination-dependent proteasomal degradation (notably of pericentrin, leading to repression of active viral chromatin during herpesvirus infection)