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[Beta]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier.

beta-Spectrin and ankyrin are major components of the membrane cytoskeleton. We have generated mice carrying a null mutation in the betaIV-spectrin gene using gene trapping in embryonic stem cells. Mice homozygous for the mutation exhibit tremors and contraction of hindlimbs. betaIV-spectrin expression is mostly restricted to neurons, where it colocalizes with and binds to ankyrin-G at axon initial segments (AISs) and nodes of Ranvier (NR). In betaIV-spectrin-null neurons, neither ankyrin-G nor voltage-gated sodium channels (VGSC) are correctly clustered at these sites, suggesting that impaired action potential caused by mislocalization of VGSC leads to the phenotype. Conversely, in ankyrin-G-null neurons, betaIV-spectrin is not localized to these sites. These results indicate that betaIV-spectrin and ankyrin-G mutually stabilize the membrane protein cluster and the linked membrane cytoskeleton at AIS and NR.

Pubmed ID: 11807096


  • Komada M
  • Soriano P


The Journal of cell biology

Publication Data

January 21, 2002

Associated Grants

  • Agency: NICHD NIH HHS, Id: HD24875

Mesh Terms

  • Animals
  • Ankyrins
  • Axons
  • Base Sequence
  • Brain
  • Cells, Cultured
  • Cytoskeleton
  • Gene Deletion
  • Gene Expression Profiling
  • Hindlimb
  • Ion Channel Gating
  • Mice
  • Mice, Knockout
  • Mice, Mutant Strains
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Phenotype
  • Protein Isoforms
  • Protein Transport
  • RNA, Messenger
  • Ranvier's Nodes
  • Retroviridae
  • Sodium Channels
  • Spectrin
  • Tremor