ATAXIN-2 intermediate-length polyglutamine expansions elicit ALS-associated metabolic and immune phenotypes

Nat Commun. 2024 Aug 29;15(1):7484. doi: 10.1038/s41467-024-51676-0.

Abstract

Intermediate-length repeat expansions in ATAXIN-2 (ATXN2) are the strongest genetic risk factor for amyotrophic lateral sclerosis (ALS). At the molecular level, ATXN2 intermediate expansions enhance TDP-43 toxicity and pathology. However, whether this triggers ALS pathogenesis at the cellular and functional level remains unknown. Here, we combine patient-derived and mouse models to dissect the effects of ATXN2 intermediate expansions in an ALS background. iPSC-derived motor neurons from ATXN2-ALS patients show altered stress granules, neurite damage and abnormal electrophysiological properties compared to healthy control and other familial ALS mutations. In TDP-43Tg-ALS mice, ATXN2-Q33 causes reduced motor function, NMJ alterations, neuron degeneration and altered in vitro stress granule dynamics. Furthermore, gene expression changes related to mitochondrial function and inflammatory response are detected and confirmed at the cellular level in mice and human neuron and organoid models. Together, these results define pathogenic defects underlying ATXN2-ALS and provide a framework for future research into ATXN2-dependent pathogenesis and therapy.

MeSH terms

  • Amyotrophic Lateral Sclerosis* / genetics
  • Amyotrophic Lateral Sclerosis* / metabolism
  • Amyotrophic Lateral Sclerosis* / pathology
  • Animals
  • Ataxin-2* / genetics
  • Ataxin-2* / metabolism
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Disease Models, Animal*
  • Female
  • Humans
  • Induced Pluripotent Stem Cells* / metabolism
  • Male
  • Mice
  • Mice, Transgenic*
  • Mitochondria / metabolism
  • Motor Neurons* / metabolism
  • Motor Neurons* / pathology
  • Neurites / metabolism
  • Peptides* / genetics
  • Peptides* / metabolism
  • Phenotype

Substances

  • Ataxin-2
  • Peptides
  • polyglutamine
  • ATXN2 protein, human
  • DNA-Binding Proteins