Mutations in alpha-tubulin cause abnormal neuronal migration in mice and lissencephaly in humans

Cell. 2007 Jan 12;128(1):45-57. doi: 10.1016/j.cell.2006.12.017.

Abstract

The development of the mammalian brain is dependent on extensive neuronal migration. Mutations in mice and humans that affect neuronal migration result in abnormal lamination of brain structures with associated behavioral deficits. Here, we report the identification of a hyperactive N-ethyl-N-nitrosourea (ENU)-induced mouse mutant with abnormalities in the laminar architecture of the hippocampus and cortex, accompanied by impaired neuronal migration. We show that the causative mutation lies in the guanosine triphosphate (GTP) binding pocket of alpha-1 tubulin (Tuba1) and affects tubulin heterodimer formation. Phenotypic similarity with existing mouse models of lissencephaly led us to screen a cohort of patients with developmental brain anomalies. We identified two patients with de novo mutations in TUBA3, the human homolog of Tuba1. This study demonstrates the utility of ENU mutagenesis in the mouse as a means to discover the basis of human neurodevelopmental disorders.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anxiety / genetics
  • Anxiety / pathology
  • Behavior, Animal
  • Cell Movement*
  • Cerebral Cortex / abnormalities*
  • Cerebral Cortex / pathology
  • Chromosome Mapping
  • DNA Mutational Analysis
  • Dimerization
  • Female
  • Glutamic Acid / genetics
  • Guanosine Triphosphate / metabolism
  • Hippocampus / abnormalities*
  • Hippocampus / pathology
  • Humans
  • Male
  • Memory Disorders / genetics
  • Memory Disorders / pathology
  • Mice
  • Mice, Mutant Strains
  • Molecular Sequence Data
  • Mutation / genetics*
  • Neurons / pathology*
  • Phenotype
  • Serine / genetics
  • Tubulin / chemistry
  • Tubulin / genetics*
  • Tubulin / metabolism*

Substances

  • Tubulin
  • Glutamic Acid
  • Serine
  • Guanosine Triphosphate