Title

Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits

UMMS Affiliation

Department of Cell Biology and Program in Neuroscience

Date

4-30-2003

Document Type

Article

Subjects

Amino Acid Motifs; Amino Acid Sequence; Animals; Ankyrins; Cell Adhesion Molecules; Cell Line; Cell Membrane; Cells, Cultured; Cricetinae; DNA, Complementary; Hippocampus; Microscopy, Fluorescence; Molecular Sequence Data; Nerve Growth Factors; Neurons; Plasmids; Protein Binding; Protein Structure, Tertiary; Rats; Rats, Wistar; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Sodium Channels; Transfection; Two-Hybrid System Techniques

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

Interactions with ankyrinG are crucial to the localization of voltage-gated sodium channels (VGSCs) at the axon initial segment and for neurons to initiate action potentials. However, the molecular nature of these interactions remains unclear. Here we report that VGSC-alpha, but not -beta, subunits bind to ankyrinG using pull-down assays. Further dissection of this activity identifies a conserved 9-amino acid motif ((V/A)P(I/L)AXXE(S/D)D) required for ankyrinG binding. This motif is also required for the localization of chimeric neurofascin/sodium channel molecules to the initial segment of cultured hippocampal neurons. The conserved nature of this motif suggests that it functions to localize sodium channels to a variety of "excitable" membrane domains both inside and outside of the nervous system.

Rights and Permissions

Citation: J Biol Chem. 2003 Jul 25;278(30):27333-9. Epub 2003 Apr 25. Link to article on publisher's site

DOI of Published Version

10.1074/jbc.M303327200

Related Resources

Link to Article in PubMed

Journal Title

The Journal of biological chemistry

PubMed ID

12716895