The Glycosylphosphatidyl Inositol-anchored Adhesion Molecule F3/Contactin Is Required for Surface Transport of Paranodin/Contactin-associated Protein (caspr)

doi:10.1083/jcb.149.2.491

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© The Rockefeller University Press, 0021-9525/2000/4/491/ $5.00
The Journal of Cell Biology, Volume 149, Number 2, April 17, 2000 491-502

Original Article

The Glycosylphosphatidyl Inositol-anchored Adhesion Molecule F3/Contactin Is Required for Surface Transport of Paranodin/Contactin-associated Protein (caspr)

Catherine Faivre-Sarrailh^a, France Gauthier^a, Natalia Denisenko-Nehrbass^b, André Le Bivic^a, Geneviève Rougon^a, and Jean-Antoine Girault^b
^a Laboratoire de Génétique et Physiologie du Développement, UMR 6545 CNRS, IBDM, 13288 Marseille, France
^b Institut National de la Santé et de la Recherche Médicale (INSERM) U563 and INSERM U114, Collège de France, 75231 Paris, France

Correspondence to: Catherine Faivre-Sarrailh, Laboratoire de Génétique et de Physiologie du Développement, UMR 6545 CNRS, IBDM, Parc Scientifique de Luminy, 13288 Marseille cedex 9, France. Tel:33-4-9126-9736 Fax:33-4-9126-9748 E-mail:sarrailh{at}lgpd.univ-mrs.fr.

Paranodin/contactin-associated protein (caspr) is a transmembraneglycoprotein of the neurexin superfamily that is highly enrichedin the paranodal regions of myelinated axons. We have investigatedthe role of its association with F3/contactin, a glycosylphosphatidylinositol (GPI)-anchored neuronal adhesion molecule of the Igsuperfamily. Paranodin was not expressed at the cell surfacewhen transfected alone in CHO or neuroblastoma cells. Cotransfectionwith F3 resulted in plasma membrane delivery of paranodin, asanalyzed by confocal microscopy and cell surface biotinylation.The region that mediates association with paranodin was mappedto the Ig domains of F3 by coimmunoprecipitation experiments.The association of paranodin with F3 allowed its recruitmentto Triton X-100–insoluble microdomains. The GPI anchorof F3 was necessary, but not sufficient for surface expressionof paranodin. F3-Ig, a form of F3 deleted of the fibronectintype III (FNIII) repeats, although GPI-linked and expressedat the cell surface, was not recovered in the microdomain fractionand was unable to promote cell surface targeting of paranodin.Thus, a cooperative effect between the GPI anchor, the FNIIIrepeats, and the Ig regions of F3 is required for recruitmentof paranodin into lipid rafts and its sorting to the plasmamembrane.

Key Words: neurexin, GPI anchor, lipid rafts, myelination, node of Ranvier

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