ArticleThe Journal of cell biology2000
The glycosylphosphatidyl inositol-anchored adhesion molecule F3/contactin is required for surface transport of paranodin/contactin-associated protein (caspr).
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Glycans and Carbohydrate-Binding/Transforming Proteins in Axon Physiology.Advances in neurobiology · 2023Article
- Value of Antibody Determinations in Chronic Dysimmune Neuropathies.Brain sciences · 2022Review
- One Raft to Guide Them All, and in Axon Regeneration Inhibit Them.International journal of molecular sciences · 2021Review
- Assembly and Function of the Juxtaparanodal Kv1 Complex in Health and Disease.Life (Basel, Switzerland) · 2020Review
- Independent anterograde transport and retrograde cotransport of domain components of myelinated axons.The Journal of cell biology · 2020Article
- Contactins in the central nervous system: role in health and disease.Neural regeneration research · 2019Review
- Caspr1 is a host receptor for meningitis-causing Escherichia coli.Nature communications · 2018Article
- Neurons define non-myelinated axon segments by the regulation of galectin-4-containing axon membrane domains.Scientific reports · 2017Article
- The sugar code in neuronal physiology.Histochemistry and cell biology · 2017Review
- Structural Characterization of the Extracellular Domain of CASPR2 and Insights into Its Association with the Novel Ligand Contactin1.The Journal of biological chemistry · 2016Article
- Myelin-associated glycoprotein gene mutation causes Pelizaeus-Merzbacher disease-like disorder.Brain : a journal of neurology · 2015Article
- Specific contactin N-glycans are implicated in neurofascin binding and autoimmune targeting in peripheral neuropathies.The Journal of biological chemistry · 2014Article
- Contactin-1 regulates myelination and nodal/paranodal domain organization in the central nervous system.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Neuro-glial interactions at the nodes of Ranvier: implication in health and diseases.Frontiers in cellular neuroscience · 2013Review
- Organization and maintenance of molecular domains in myelinated axons.Journal of neuroscience research · 2013Review
- Receptor-like protein-tyrosine phosphatase α enhances cell surface expression of neural adhesion molecule NB-3.The Journal of biological chemistry · 2011Article
- The expression of TAG-1 in glial cells is sufficient for the formation of the juxtaparanodal complex and the phenotypic rescue of tag-1 homozygous mutants in the CNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Cellular form of prion protein inhibits Reelin-mediated shedding of Caspr from the neuronal cell surface to potentiate Caspr-mediated inhibition of neurite outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Thrombospondin 1--a key astrocyte-derived neurogenic factor.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010Article
- Lewis(x) and alpha2,3-sialyl glycans and their receptors TAG-1, Contactin, and L1 mediate CD24-dependent neurite outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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