RGD Reference Report - Structures, alternative splicing, and neurexin binding of multiple neuroligins. - Rat Genome Database

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Structures, alternative splicing, and neurexin binding of multiple neuroligins.

Authors: Ichtchenko, K  Nguyen, T  Sudhof, TC 
Citation: Ichtchenko K, etal., J Biol Chem 1996 Feb 2;271(5):2676-82.
RGD ID: 729051
Pubmed: PMID:8576240   (View Abstract at PubMed)

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 Sudhof, 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 beta-neurexins both as native brain proteins and as recombinant proteins. Tight binding of the three neuroligins to beta-neurexins is observed only for beta-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.

Objects referenced in this article
Gene Nlgn1 neuroligin 1 Rattus norvegicus
Gene Nlgn2 neuroligin 2 Rattus norvegicus
Gene Nlgn3 neuroligin 3 Rattus norvegicus
Gene Nrxn1 neurexin 1 Rattus norvegicus
Gene Nrxn2 neurexin 2 Rattus norvegicus
Gene Nrxn3 neurexin 3 Rattus norvegicus

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