TRIM37 is a primate-specific E3 ligase for Huntingtin and accounts for the striatal degeneration in Huntington's disease

Sci Adv. 2024 May 17;10(20):eadl2036. doi: 10.1126/sciadv.adl2036. Epub 2024 May 17.

Abstract

Huntington's disease (HD) is an autosomal dominant neurodegenerative disease characterized by preferential neuronal loss in the striatum. The mechanism underlying striatal selective neurodegeneration remains unclear, making it difficult to develop effective treatments for HD. In the brains of nonhuman primates, we examined the expression of Huntingtin (HTT), the gene responsible for HD. We found that HTT protein is highly expressed in striatal neurons due to its slow degradation in the striatum. We also identified tripartite motif-containing 37 (TRIM37) as a primate-specific protein that interacts with HTT and is selectively reduced in the primate striatum. TRIM37 promotes the ubiquitination and degradation of mutant HTT (mHTT) in vitro and modulates mHTT aggregation in mouse and monkey brains. Our findings suggest that nonhuman primates are crucial for understanding the mechanisms of human diseases such as HD and support TRIM37 as a potential therapeutic target for treating HD.

MeSH terms

  • Animals
  • Corpus Striatum* / metabolism
  • Corpus Striatum* / pathology
  • Disease Models, Animal
  • Humans
  • Huntingtin Protein* / genetics
  • Huntingtin Protein* / metabolism
  • Huntington Disease* / genetics
  • Huntington Disease* / metabolism
  • Huntington Disease* / pathology
  • Mice
  • Neurons / metabolism
  • Neurons / pathology
  • Primates
  • Proteolysis
  • Tripartite Motif Proteins* / genetics
  • Tripartite Motif Proteins* / metabolism
  • Ubiquitin-Protein Ligases* / genetics
  • Ubiquitin-Protein Ligases* / metabolism
  • Ubiquitination*

Substances

  • HTT protein, human