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© The Rockefeller University Press, 0021-9525/2000//491 $5.00
The Journal of Cell Biology, Volume 149, Number 2, , 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-Sarrailha, France Gauthiera, Natalia Denisenko-Nehrbassb, André Le Bivica, Geneviève Rougona, and Jean-Antoine Giraultb

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
Laboratoire de Génétique et de Physiologie du Développement, UMR 6545 CNRS, IBDM, Parc Scientifique de Luminy, 13288 Marseille cedex 9, France.33-4-9126-974833-4-9126-9736

sarrailh{at}lgpd.univ-mrs.fr

Paranodin/contactin-associated protein (caspr) is a transmembrane glycoprotein of the neurexin superfamily that is highly enriched in the paranodal regions of myelinated axons. We have investigated the role of its association with F3/contactin, a glycosylphosphatidyl inositol (GPI)-anchored neuronal adhesion molecule of the Ig superfamily. Paranodin was not expressed at the cell surface when transfected alone in CHO or neuroblastoma cells. Cotransfection with F3 resulted in plasma membrane delivery of paranodin, as analyzed by confocal microscopy and cell surface biotinylation. The region that mediates association with paranodin was mapped to the Ig domains of F3 by coimmunoprecipitation experiments. The association of paranodin with F3 allowed its recruitment to Triton X-100–insoluble microdomains. The GPI anchor of F3 was necessary, but not sufficient for surface expression of paranodin. F3-Ig, a form of F3 deleted of the fibronectin type III (FNIII) repeats, although GPI-linked and expressed at the cell surface, was not recovered in the microdomain fraction and was unable to promote cell surface targeting of paranodin. Thus, a cooperative effect between the GPI anchor, the FNIII repeats, and the Ig regions of F3 is required for recruitment of paranodin into lipid rafts and its sorting to the plasma membrane.

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

© 2000 The Rockefeller University Press

Abbreviations used in this paper: CAM, cell adhesion molecule; caspr, contactin-associated protein; EGF, epidermal growth factor; FNIII, fibronectin type III; GNP, glycophorin C, neurexin IV, paranodin motif; GPI, glycosylphosphatidyl inositol; PI-PLC, phosphatidyl inositol-phospholipase C; TX-100, Triton X-100.


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