GPI-anchored proteins at the node of Ranvier

FEBS Lett. 2010 May 3;584(9):1787-92. doi: 10.1016/j.febslet.2009.08.025. Epub 2009 Aug 22.


Contactin and TAG-1 are glycan phosphatidyl inositol (GPI)-anchored cell adhesion molecules that play a crucial role in the organization of axonal subdomains at the node of Ranvier of myelinating fibers. Contactin and TAG-1 mediate axo-glial selective interactions in association with Caspr-family molecules at paranodes and juxtaparanodes, respectively. How membrane proteins can be confined in these neighbouring domains along the axon has been the subject of intense investigations. This review will specifically examine the properties conferred by the lipid microenvironment to regulate trafficking and selective association of these axo-glial complexes. Increasing evidences from genetic and neuropathological models point to a role of lipid rafts in the formation or stabilization of the paranodal junctions.

Publication types

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

MeSH terms

  • Animals
  • Axons / chemistry
  • Axons / metabolism
  • Biological Transport / physiology
  • Glycosylphosphatidylinositols / metabolism*
  • Humans
  • Intercellular Junctions / metabolism
  • Intercellular Junctions / physiology
  • Membrane Microdomains / metabolism
  • Membrane Microdomains / physiology
  • Membrane Proteins / metabolism*
  • Membrane Proteins / physiology
  • Models, Biological
  • Ranvier's Nodes / metabolism*
  • Ranvier's Nodes / physiology


  • Glycosylphosphatidylinositols
  • Membrane Proteins