Tripartite motif-containing protein 37 (TRIM37)

Tripartite motif-containing protein 37 (TRIM37) is an E3 ubiquitin ligase and a member of the TRIM family of proteins, characterized by RING, B-box, and coiled-coil domains[1][5]. TRIM37 catalyzes ubiquitination of specific substrate proteins, including histone H2A, modulating transcriptional repression of tumor suppressor genes, and regulates protein assemblies at centrosomes and spindle poles to ensure proper cell division and chromosomal segregation[1][2][3][4]. Germline mutations result in Mulibrey nanism, a multisystem developmental disorder associated with high tumor risk, while somatic copy number gain or overexpression of TRIM37 is linked to aggressive forms of breast cancer and neuroblastoma[1][3][4]. Elevated TRIM37 sensitizes cells to centrinone—a PLK4 inhibitor—providing a potential therapeutic vulnerability in cancer[3]. Loss or dysregulation of this protein is associated with centrosomal abnormalities, genome instability, and altered transcriptional landscapes promoting oncogenesis[1][2][3][4][5].

Other names

E3 ubiquitin-protein ligase TRIM37KIAA0898MULPOB1TEF3Mulibrey nanism proteinRING-type E3 ubiquitin transferase TRIM37RING-B-box-coiled-coil protein

Centrinone: inhibits PLK4, targeting cells bearing excess TRIM37 and with aberrant centrosome numbers[3]