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MBC in Press, published online ahead of print November 8, 2006
Mol. Biol. Cell 10.1091/mbc.E06-06-0570

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Submitted on June 30, 2006
Revised on October 2, 2006
Accepted on October 30, 2006

PGY Repeats and N-Glycans Govern the Trafficking of Paranodin and Its Selective Association with Contactin and Neurofascin-155

Carine Bonnon,* Christophe Bel,* Laurence Goutebroze,{dagger} Bernard Maigret,{ddagger} Jean-Antoine Girault,{dagger} and Catherine Faivre-Sarrailh*

*Neurobiologie des Interactions Cellulaires et Neurophysiopathologie, CNRS UMR 6184, Université de la Méditerranée, Institut Jean-Roche, 13916 Marseille Cedex 20, France; {dagger}INSERM and Université Pierre et Marie Curie (UPMC-Paris 6), and Institut du Fer à Moulin, Paris F-75005, France; {ddagger}Equipe de Dynamique des Assemblages Membranaires, CNRS UMR 7565, Université Henri Poincaré, F-54506 Vandoeuvre-les-Nancy, France

Monitoring Editor: Jeffrey Brodsky

Formation of nodes of Ranvier requires contact of axons with myelinating glial cells, generating specialized axo-glial subdomains. Caspr/paranodin is required for the formation of septate-like junctions at paranodes, while the related caspr2 is essential for the organization of juxtaparanodes. The molecular mechanisms underlying the segregation of these related glycoproteins within distinct complexes are poorly understood. Exit of paranodin from the endoplasmic reticulum (ER) is mediated by its interaction with F3/contactin. Using domain swapping with caspr2, we mapped a motif with ProGly-Tyr repeats (PGY) in the ectodomain of paranodin responsible for its ER retention. Deletion of PGY allows cell surface delivery of paranodin by-passing the calnexin-calreticulin quality control. Conversely, insertion of PGY in caspr2 or NrCAM blocks these proteins in the ER. PGY is a novel type of processing signal that compels chaperoning of paranodin by contactin. Contactin associated with paranodin is expressed at the cell surface with high-mannose N-glycans. Using mutant CHO lines altered in the processing of N-linked carbohydrates, we show that the high-mannose glycoform of contactin strongly binds neurofascin-155, its glial partner at paranodes. Thus, the unconventional processing of paranodin and contactin may determine the selective association of axo-glial complexes at paranodes.

Address correspondence to: Catherine Faivre-Sarrailh (sarrailh.c{at}jean-roche.univ-mrs.fr)




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