Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions.

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.
Mesh Terms:
Amino Acid Sequence, Animals, Blotting, Western, Cell Adhesion Molecules, Neuronal, Cell Membrane, Cloning, Molecular, Gene Expression, Humans, Immunohistochemistry, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Protein Binding, RNA, Messenger, Rats, Receptors, Cell Surface, Recombinant Fusion Proteins, Sequence Alignment, Signal Transduction, Tumor Cells, Cultured, src Homology Domains
EMBO J.
Date: Mar. 03, 1997
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