C9ORF72 GGGGCC repeat-associated non-AUG translation is upregulated by stress through eIF2α phosphorylation

Nat Commun. 2018 Jan 4;9(1):51. doi: 10.1038/s41467-017-02495-z.

Abstract

Hexanucleotide repeat expansion in C9ORF72 is the most frequent cause of both amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Here we demonstrate that the repeat-associated non-AUG (RAN) translation of (GGGGCC) n -containing RNAs into poly-dipeptides can initiate in vivo without a 5'-cap. The primary RNA substrate for RAN translation of C9ORF72 sense repeats is shown to be the spliced first intron, following its excision from the initial pre-mRNA and transport to the cytoplasm. Cap-independent RAN translation is shown to be upregulated by various stress stimuli through phosphorylation of the α subunit of eukaryotic initiation factor-2 (eIF2α), the core event of an integrated stress response (ISR). Compounds inhibiting phospho-eIF2α-signaling pathways are shown to suppress RAN translation. Since the poly-dipeptides can themselves induce stress, these findings support a feedforward loop with initial repeat-mediated toxicity enhancing RAN translation and subsequent production of additional poly-dipeptides through ISR, thereby promoting progressive disease.

Publication types

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

MeSH terms

  • Amyotrophic Lateral Sclerosis / genetics
  • C9orf72 Protein / genetics*
  • C9orf72 Protein / metabolism
  • DNA Repeat Expansion
  • Dipeptides
  • Eukaryotic Initiation Factor-2 / metabolism*
  • Feedback, Physiological
  • Frontotemporal Dementia / genetics
  • HeLa Cells
  • Humans
  • Introns
  • Peptides
  • Phosphorylation
  • Protein Biosynthesis
  • RNA Splicing
  • Stress, Physiological / genetics*
  • Up-Regulation

Substances

  • C9orf72 Protein
  • C9orf72 protein, human
  • Dipeptides
  • Eukaryotic Initiation Factor-2
  • Peptides