Structures, Alternative Splicing, and Neurexin Binding of Multiple Neuroligins ()

Neuroligin 1 is a neuronal cell surface protein that binds to a subset of neurexins, polymorphic cell surface proteins that are also localized on neurons (Ichtchenko, K., Hata, Y., Nguyen, T., Ullrich, B., Missler, M., Moomaw, C., and Südhof, T. C. (1995) Cell 81, 435-443). We now describe two novel...

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Bibliographic Details
Published in:The Journal of biological chemistry 1996-02, Vol.271 (5), p.2676-2682
Main Authors: Ichtchenko, Konstantin, Nguyen, Thai, Südhof, Thomas C.
Format: Article
Language:English
Subjects:
Alternative Splicing
Amino Acid Sequence
Animals
Cell Adhesion Molecules, Neuronal
Cell Communication
Cell Line
DNA, Complementary
Membrane Proteins - metabolism
Molecular Sequence Data
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurons - cytology
Neurons - metabolism
Protein Binding
Sequence Homology, Amino Acid
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Summary:Neuroligin 1 is a neuronal cell surface protein that binds to a subset of neurexins, polymorphic cell surface proteins that are also localized on neurons (Ichtchenko, K., Hata, Y., Nguyen, T., Ullrich, B., Missler, M., Moomaw, C., and Südhof, T. C. (1995) Cell 81, 435-443). We now describe two novel neuroligins called neuroligins 2 and 3 that are similar in structure and sequence to neuroligin 1. All neuroligins contain an N-terminal hydrophobic sequence with the characteristics of a cleaved signal peptide followed by a large esterase homology domain, a highly conserved single transmembrane region, and a short cytoplasmic domain. The three neuroligins are alternatively spliced at the same position and are expressed at high levels only in brain. Binding studies demonstrate that all three neuroligins bind to β-neurexins both as native brain proteins and as recombinant proteins. Tight binding of the three neuroligins to β-neurexins is observed only for β-neurexins lacking an insert in splice site 4. Thus, neuroligins constitute a multigene family of brain-specific proteins with distinct isoforms that may have overlapping functions in mediating recognition processes between neurons.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.5.2676