Alsin and the molecular pathways of amyotrophic lateral sclerosis

Mol Neurobiol. 2007 Dec;36(3):224-31. doi: 10.1007/s12035-007-0034-x. Epub 2007 Jul 10.

Abstract

Autosomal recessive mutations in the ALS2 gene lead to a clinical spectrum of motor dysfunction including juvenile onset amyotrophic lateral sclerosis (ALS2), primary lateral sclerosis, and hereditary spastic paraplegia. The 184-kDa alsin protein, encoded by the full-length ALS2 gene, contains three different guanine-nucleotide-exchange factor-like domains, which may play a role in the etiology of the disease. Multiple in vitro biochemical and cell biology assays suggest that alsin dysfunction affects endosome trafficking through a Rab5 small GTPase family-mediated mechanism. Four ALS2-deficient mouse models have been generated by different groups and used to study the behavioral and pathological impact of alsin deficiency. These mouse models largely fail to recapitulate hallmarks of motor neuron disease, but the subtle deficits that are observed in behavior and pathology have aided in our understanding of the relationship between alsin and motor dysfunction. In this review, we summarize recent clinical and molecular reports regarding alsin and attempt to place these results within the larger context of motor neuron disease.

Publication types

  • Research Support, N.I.H., Intramural
  • Review

MeSH terms

  • Animals
  • Guanine Nucleotide Exchange Factors / chemistry
  • Guanine Nucleotide Exchange Factors / genetics*
  • Humans
  • Mice
  • Mice, Knockout
  • Models, Molecular
  • Motor Neuron Disease / genetics*
  • Motor Neurons / physiology*
  • Mutation
  • Polymorphism, Single Nucleotide
  • Protein Conformation
  • Sequence Deletion
  • Spastic Paraplegia, Hereditary / genetics*

Substances

  • ALS2 protein, human
  • Als2 protein, mouse
  • Guanine Nucleotide Exchange Factors