The Glycosylphosphatidyl Inositol-Anchored Adhesion Molecule F3/Contactin Is Required for Surface Transport of Paranodin/Contactin-Associated Protein (Caspr)

Autor: Catherine Faivre-Sarrailh, France Gauthier, Natalia Denisenko-Nehrbass, André Le Bivic, Geneviève Rougon, Jean-Antoine Girault
Přispěvatelé: Khrestchatisky, Michel, Neurobiologie des interactions cellulaires et neurophysiopathologie - NICN (NICN), Université de la Méditerranée - Aix-Marseille 2-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2000
Předmět:
Models
Molecular
Repetitive Sequences
Amino Acid
node of Ranvier
Immunoprecipitation
Glycosylphosphatidylinositols
Protein Conformation
Cell Adhesion Molecules
Neuronal
Recombinant Fusion Proteins
Golgi Apparatus
Immunoglobulin domain
CHO Cells
Biology
Transfection
Cell membrane
neurexin
Neuroblastoma
Contactins
Paranodal junction
Cricetinae
medicine
Tumor Cells
Cultured
Animals
Humans
[SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]
Fluorescent Antibody Technique
Indirect
Lipid raft
Sequence Deletion
lipid rafts
COS cells
GPI anchor
Membrane Glycoproteins
Cell adhesion molecule
Lipid microdomain
Cell Membrane
Neuropeptides
myelination
Cell Biology
Cell biology
medicine.anatomical_structure
COS Cells
Mutagenesis
Site-Directed
[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]
Original Article
Zdroj: The Journal of Cell Biology
Journal of Cell Biology
Journal of Cell Biology, 2000, 149(2), pp.491-502
ISSN: 1540-8140
0021-9525
Popis: 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.
Databáze: OpenAIRE
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