Reeler: new tales on an old mutant mouse

Bioessays. 1998 Mar;20(3):235-44. doi: 10.1002/(SICI)1521-1878(199803)20:3<235::AID-BIES7>3.0.CO;2-Q.


Neurological mouse mutants provide an opportunity to dissect the complex mechanisms that underlie vertebrate brain development. Advances in genetic technologies have permitted the identification of genes disrupted in many mutants, allowing a molecular interpretation of the phenotypes. For several decades, the spontaneous mutant mouse reeler has been used as a model for the analysis of the development of laminated brain structures. In this ataxic mutant, the migration of many neurons is aberrant, resulting in disrupted cellular organization. Recently, reelin, the gene disrupted in the reeler mouse, has been identified, reelin encodes a novel extracellular molecule that controls neural cell positioning through mechanisms that are not yet completely understood. Analysis of the expression pattern and the properties of the reelin gene product (Reelin) suggests models for its function during brain development. Furthermore, the recent identification of genes that may function in the Reelin signaling pathway advances our knowledge of the molecular basis of neuronal migration.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Brain / growth & development*
  • Cell Adhesion Molecules, Neuronal / biosynthesis
  • Cell Adhesion Molecules, Neuronal / genetics*
  • Chromosome Mapping
  • Chromosomes, Human, Pair 7
  • Extracellular Matrix Proteins / biosynthesis
  • Extracellular Matrix Proteins / genetics*
  • Humans
  • Mice
  • Mice, Neurologic Mutants / genetics*
  • Nerve Tissue Proteins / biosynthesis
  • Nerve Tissue Proteins / genetics
  • Nervous System Diseases / genetics*
  • Reelin Protein
  • Serine Endopeptidases


  • Cell Adhesion Molecules, Neuronal
  • Extracellular Matrix Proteins
  • Nerve Tissue Proteins
  • Reelin Protein
  • RELN protein, human
  • Reln protein, mouse
  • Serine Endopeptidases