ALS-associated mutant FUS induces selective motor neuron degeneration through toxic gain of function

Nat Commun. 2016 Feb 4:7:10465. doi: 10.1038/ncomms10465.

Abstract

Mutations in FUS cause amyotrophic lateral sclerosis (ALS), including some of the most aggressive, juvenile-onset forms of the disease. FUS loss-of-function and toxic gain-of-function mechanisms have been proposed to explain how mutant FUS leads to motor neuron degeneration, but neither has been firmly established in the pathogenesis of ALS. Here we characterize a series of transgenic FUS mouse lines that manifest progressive, mutant-dependent motor neuron degeneration preceded by early, structural and functional abnormalities at the neuromuscular junction. A novel, conditional FUS knockout mutant reveals that postnatal elimination of FUS has no effect on motor neuron survival or function. Moreover, endogenous FUS does not contribute to the onset of the ALS phenotype induced by mutant FUS. These findings demonstrate that FUS-dependent motor degeneration is not due to loss of FUS function, but to the gain of toxic properties conferred by ALS mutations.

Publication types

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

MeSH terms

  • Amyotrophic Lateral Sclerosis / genetics*
  • Animals
  • Cell Survival / genetics
  • Disease Models, Animal
  • Humans
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Microscopy, Confocal
  • Microscopy, Electron
  • Motor Neurons / metabolism*
  • Muscle, Skeletal / innervation
  • Muscle, Skeletal / pathology*
  • Mutation
  • Nerve Degeneration / genetics*
  • Nerve Degeneration / pathology
  • Neuromuscular Junction / metabolism*
  • Phenotype
  • RNA-Binding Protein FUS / genetics*
  • Spinal Cord / metabolism
  • Spinal Cord / pathology*

Substances

  • FUS protein, human
  • RNA-Binding Protein FUS