Transcriptional dysregulation by a nucleus-localized aminoacyl-tRNA synthetase associated with Charcot-Marie-Tooth neuropathy

Nat Commun. 2019 Nov 6;10(1):5045. doi: 10.1038/s41467-019-12909-9.

Abstract

Charcot-Marie-Tooth disease (CMT) is a length-dependent peripheral neuropathy. The aminoacyl-tRNA synthetases constitute the largest protein family implicated in CMT. Aminoacyl-tRNA synthetases are predominantly cytoplasmic, but are also present in the nucleus. Here we show that a nuclear function of tyrosyl-tRNA synthetase (TyrRS) is implicated in a Drosophila model of CMT. CMT-causing mutations in TyrRS induce unique conformational changes, which confer capacity for aberrant interactions with transcriptional regulators in the nucleus, leading to transcription factor E2F1 hyperactivation. Using neuronal tissues, we reveal a broad transcriptional regulation network associated with wild-type TyrRS expression, which is disturbed when a CMT-mutant is expressed. Pharmacological inhibition of TyrRS nuclear entry with embelin reduces, whereas genetic nuclear exclusion of mutant TyrRS prevents hallmark phenotypes of CMT in the Drosophila model. These data highlight that this translation factor may contribute to transcriptional regulation in neurons, and suggest a therapeutic strategy for CMT.

Publication types

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

MeSH terms

  • Amino Acyl-tRNA Synthetases / genetics
  • Amino Acyl-tRNA Synthetases / metabolism*
  • Animals
  • Animals, Genetically Modified
  • Behavior, Animal
  • Cell Nucleus / enzymology
  • Cell Nucleus / metabolism*
  • Charcot-Marie-Tooth Disease / genetics
  • Charcot-Marie-Tooth Disease / metabolism*
  • Disease Models, Animal
  • Drosophila
  • Drosophila Proteins / metabolism
  • Female
  • Genetic Predisposition to Disease*
  • HEK293 Cells
  • Humans
  • Larva
  • Male
  • Mutation
  • Nervous System Diseases
  • Neuromuscular Junction
  • Neurons / metabolism
  • Phenotype
  • Transcription Factors / metabolism

Substances

  • Drosophila Proteins
  • E2f1 protein, Drosophila
  • Transcription Factors
  • Amino Acyl-tRNA Synthetases