Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.

Journal Article (Journal Article)

AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network. This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms. The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides. AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination. The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates. Immunofluorescence revealed co-localization of ankyrinG and O-GlcNAc immunoreactivity at nodes of Ranvier. These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.

Full Text

Duke Authors

Cited Authors

  • Zhang, X; Bennett, V

Published Date

  • December 6, 1996

Published In

Volume / Issue

  • 271 / 49

Start / End Page

  • 31391 - 31398

PubMed ID

  • 8940148

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.271.49.31391


  • eng

Conference Location

  • United States