Misregulated RNA processing in amyotrophic lateral sclerosis

Brain Res. 2012 Jun 26:1462:3-15. doi: 10.1016/j.brainres.2012.02.059. Epub 2012 Mar 3.

Abstract

Amyotrophic lateral sclerosis (ALS) research is undergoing an era of unprecedented discoveries with the identification of new genes as major genetic causes of this disease. These discoveries reinforce the genetic, clinical and pathological overlap between ALS and frontotemporal lobar degeneration (FTLD). Common causes of these diseases include mutations in the RNA/DNA-binding proteins, TDP-43 and FUS/TLS and most recently, hexanucleotide expansions in the C9orf72 gene, discoveries that highlight the overlapping pathogenic mechanisms that trigger ALS and FTLD. TDP-43 and FUS/TLS, both of which participate in several steps of RNA processing, are abnormally aggregated and mislocalized in ALS and FTLD, while the expansion in the C9orf72 pre-mRNA strongly suggests sequestration of one or more RNA binding proteins in pathologic RNA foci. Hence, ALS and FTLD converge in pathogenic pathways disrupting the regulation of RNA processing. This article is part of a Special Issue entitled RNA-Binding Proteins.

Publication types

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

MeSH terms

  • Amyotrophic Lateral Sclerosis / genetics*
  • Amyotrophic Lateral Sclerosis / metabolism
  • Animals
  • DNA-Binding Proteins / genetics
  • Frontotemporal Lobar Degeneration / genetics
  • Homeostasis
  • Humans
  • RNA / genetics*
  • RNA / metabolism
  • RNA-Binding Protein FUS / genetics
  • RNA-Binding Protein FUS / metabolism
  • RNA-Binding Proteins / genetics
  • TDP-43 Proteinopathies / genetics
  • TDP-43 Proteinopathies / pathology

Substances

  • DNA-Binding Proteins
  • RNA-Binding Protein FUS
  • RNA-Binding Proteins
  • RNA