TRIM37: a critical orchestrator of centrosome function

Cell Cycle. 2021 Dec;20(23):2443-2451. doi: 10.1080/15384101.2021.1988289. Epub 2021 Oct 21.


Loss of function mutations in the E3 ubiquitin ligase TRIM37 result in MULIBREY nanism, a disease characterized by impaired organ growth and a high propensity to develop different tumor types. Additionally, increased copy number of TRIM37 is a feature of some breast cancers and neuroblastomas. The molecular role played by TRIM37 in such loss and gain of function conditions has been a focus of research in the last decade, which led notably to the identification of critical roles of TRIM37 in centrosome biology. Specifically, deletion of TRIM37 results in the formation of aberrant centrosomal proteins assemblies, including Centrobin-PLK4 assemblies, which can act as extra MTOCs, thus resulting in defective chromosome segregation. Additionally, TRIM37 overexpression targets the centrosomal protein CEP192 for degradation, thereby preventing centrosome maturation and increasing the frequency of mitotic errors. Interestingly, increased TRIM37 protein levels sensitize cells to the PLK4 inhibitor centrinone. In this review, we cover the emerging roles of TRIM37 in centrosome biology and discuss how this knowledge may lead to new therapeutic strategies to target specific cancer cells.

Keywords: 17q23; CEP192; Centrobin; PLK4; TRIM37; centrosome; mulibrey nanism.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Centrosome / metabolism
  • Chromosomal Proteins, Non-Histone / metabolism
  • Humans
  • Microtubule-Organizing Center / metabolism
  • Mulibrey Nanism* / genetics
  • Mulibrey Nanism* / metabolism
  • Protein Serine-Threonine Kinases
  • Tripartite Motif Proteins / genetics
  • Tripartite Motif Proteins / metabolism
  • Ubiquitin-Protein Ligases* / genetics
  • Ubiquitin-Protein Ligases* / metabolism


  • Cep192 protein, human
  • Chromosomal Proteins, Non-Histone
  • Tripartite Motif Proteins
  • TRIM37 protein, human
  • Ubiquitin-Protein Ligases
  • PLK4 protein, human
  • Protein Serine-Threonine Kinases