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GPI‐anchored proteins at the node of Ranvier
Author(s) -
Labasque Marilyne,
Faivre-Sarrailh Catherine
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.08.025
Subject(s) - node of ranvier , microbiology and biotechnology , cell adhesion molecule , lipid raft , glycan , axon , membrane protein , chemistry , biophysics , biology , myelin , neuroscience , membrane , biochemistry , signal transduction , glycoprotein , central nervous system
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.