The Paranodal Complex of F3/Contactin and Caspr/Paranodin Traffics to the Cell Surface via a Non-conventional Pathway

During myelination, membrane-specialized domains are generated by complex interactions between axon and glial cells. The cell adhesion molecules caspr/paranodin and F3/contactin play a crucial role in the generation of functional septate-like junctions at paranodes. We have previously demonstrated t...

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Veröffentlicht in:	The Journal of biological chemistry 2003-11, Vol.278 (48), p.48339-48347
Hauptverfasser:	Bonnon, Carine, Goutebroze, Laurence, Denisenko-Nehrbass, Natasha, Girault, Jean-Antoine, Faivre-Sarrailh, Catherine
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Axons - metabolism Biotinylation Brain - metabolism Brefeldin A - pharmacology CD4 Antigens - biosynthesis Cell Adhesion Cell Adhesion Molecules, Neuronal - chemistry Cell Adhesion Molecules, Neuronal - metabolism Cell Line, Tumor Cell Membrane - metabolism CHO Cells Cloning, Molecular Contactins COS Cells Cricetinae Cytoplasm - metabolism Endoplasmic Reticulum - metabolism Glycosylation Golgi Apparatus - metabolism Green Fluorescent Proteins Lectins - metabolism Life Sciences Luminescent Proteins - metabolism Membrane Microdomains Mice Microscopy, Fluorescence Neurobiology Neurons and Cognition Precipitin Tests Protein Binding Protein Structure, Tertiary Protein Synthesis Inhibitors - pharmacology Protein Transport Rats Time Factors Tunicamycin - pharmacology
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