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Identification of a novel contactin‐associated transmembrane receptor with multiple domains implicated in protein–protein interactions
Open accessAbstract
Receptor protein tyrosine phosphatase beta (RPTPbeta) expressed on the surface of glial cells binds to the glycosylphosphatidylinositol (GPI)-anchored recognition molecule contactin on neuronal cells leading to neurite outgrowth. We describe the cloning of a novel contactin-associated transmembrane receptor (p190/Caspr) containing a mosaic of domains implicated in protein-protein interactions. The extracellular domain of Caspr contains a neurophilin/coagulation factor homology domain, a region related to fibrinogen beta/gamma, epidermal growth factor-like repeats, neurexin motifs as well as unique PGY repeats found in a molluscan adhesive protein. The cytoplasmic domain of Caspr contains a proline-rich sequence capable of binding to a subclass of SH3 domains of signaling molecules. Caspr and contactin exist as a complex in rat brain and are bound to each other by means of lateral (cis) interactions in the plasma membrane. We propose that Caspr may function as a signaling component of contactin, enabling recruitment and activation of intracellular signaling pathways in neurons. The binding of RPTPbeta to the contactin-Caspr complex could provide a mechanism for cell-cell communication between glial cells and neurons during development.
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“In comparison to Caspr, which becomes concentrated in the paranodal junctions of myelinated axons [49], BIN1 displayed patchy distribution along short segments of interdigitating processes without an apparent concentration in the nodes or the paranodal area (Fig. 4g).”
From Predominant expression of Alzheimer’s disease-associated BIN1 in mature oligodendrocytes and localization to white matter tracts (2016) · cites this paper as [49]
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Metadata
- Authors
- Peles, E., Nativ, M., Lustig, M., Grumet, M., Schilling, J., Martinez, R., Plowman, G. D., & Schlessinger, J.
- Affiliations
- NYU Langone Health (US)
- Corresponding author
- Schlessinger, Joseph
- Venue
- The EMBO Journal
- Published
- 1997-03-01
- Volume
- 16
- Issue
- 5
- Pages
- 978-988
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1169698
- OpenAlex
- W2098584548
- Cited by
- 400
- References
- 0
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 6 · 2023: 6 · 2022: 9 · 2021: 6 · 2020: 13 · 2019: 8 · 2018: 9 · 2017: 9 · 2016: 10 · 2015: 8 · 2014: 15 · 2013: 11 · 2012: 12
- FWCI
- 9.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ns021629-11)
- National Institute of Neurological Disorders and Stroke (NS21629)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- Caspr, contactin, epidermal growth factor-like repeats, SH3 domain binding, neurite outgrowth, intracellular signaling, rat brain
- MeSH terms
- Amino Acid Sequence, Animals, Cell Membrane, Cloning, Molecular, Humans, Immunohistochemistry, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Protein Binding, Receptors, Cell Surface, Recombinant Fusion Proteins, RNA, Messenger, Tumor Cells, Cultured, Blotting, Western, Signal Transduction, Cell Adhesion Molecules, Neuronal, Gene Expression, Sequence Alignment, src Homology Domains, Rats, Contactins
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