HuD impairs neuromuscular junctions and induces apoptosis in human iPSC and Drosophila ALS models

Nat Commun. 2024 Nov 7;15(1):9618. doi: 10.1038/s41467-024-54004-8.

Abstract

Defects at the neuromuscular junction (NMJ) are among the earliest hallmarks of amyotrophic lateral sclerosis (ALS). According to the "dying-back" hypothesis, NMJ disruption not only precedes but also triggers the subsequent degeneration of motoneurons in both sporadic (sALS) and familial (fALS) ALS. Using human induced pluripotent stem cells (iPSCs), we show that the RNA-binding protein HuD (ELAVL4) contributes to NMJ defects and apoptosis in FUS-ALS. HuD overexpression mimics the severe FUSP525L mutation, while its knockdown rescues the FUSP525L phenotypes. In Drosophila, neuronal overexpression of the HuD ortholog, elav, induces motor dysfunction, and its knockdown improves motor function in a FUS-ALS model. Finally, we report increased HuD levels upon oxidative stress in human motoneurons and in sALS patients with an oxidative stress signature. Based on these findings, we propose that HuD plays a role downstream of FUS mutations in fALS and in sALS related to oxidative stress.

MeSH terms

  • Amyotrophic Lateral Sclerosis* / genetics
  • Amyotrophic Lateral Sclerosis* / metabolism
  • Amyotrophic Lateral Sclerosis* / pathology
  • Animals
  • Apoptosis* / genetics
  • Disease Models, Animal*
  • Drosophila
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / genetics
  • ELAV-Like Protein 4* / genetics
  • ELAV-Like Protein 4* / metabolism
  • Female
  • Humans
  • Induced Pluripotent Stem Cells* / metabolism
  • Male
  • Motor Neurons* / metabolism
  • Motor Neurons* / pathology
  • Mutation
  • Neuromuscular Junction* / metabolism
  • Oxidative Stress
  • RNA-Binding Protein FUS* / genetics
  • RNA-Binding Protein FUS* / metabolism

Substances

  • RNA-Binding Protein FUS
  • ELAV-Like Protein 4
  • FUS protein, human
  • Drosophila Proteins