| http://purl.uniprot.org/citations/15858059 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15858059 | http://www.w3.org/2000/01/rdf-schema#comment | "Neurexins constitute a large family of highly variable cell-surface molecules that may function in synaptic transmission and/or synapse formation. Each of the three known neurexin genes encodes two major neurexin variants, alpha- and beta-neurexins, that are composed of distinct extracellular domains linked to identical intracellular sequences. Deletions of one, two, or all three alpha-neurexins in mice recently demonstrated their essential role at synapses. In multiple alpha-neurexin knock-outs, neurotransmitter release from excitatory and inhibitory synapses was severely reduced, primarily probably because voltage-dependent Ca2+ channels were impaired. It remained unclear, however, which neurexin variants actually influence exocytosis and Ca2+ channels, which domain of neurexins is required for this function, and which Ca2+-channel subtypes are regulated. Here, we show by electrophysiological recordings that transgenic neurexin 1alpha rescues the release and Ca2+-current phenotypes, whereas transgenic neurexin 1beta has no effect, indicating the importance of the extracellular sequences for the function of neurexins. Because neurexin 1alpha rescued the knock-out phenotype independent of the alpha-neurexin gene deleted, these data are consistent with a redundant function among different alpha-neurexins. In both knock-out and transgenically rescued mice, alpha-neurexins selectively affected the component of neurotransmitter release that depended on activation of N- and P/Q-type Ca2+ channels, but left L-type Ca2+ channels unscathed. Our findings indicate that alpha-neurexins represent organizer molecules in neurotransmission that regulate N- and P/Q-type Ca2+ channels, constituting an essential role at synapses that critically involves the extracellular domains of neurexins."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.org/dc/terms/identifier | "doi:10.1523/jneurosci.0497-05.2005"xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/author | "Zhang W."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/author | "Hammer R.E."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/author | "Sudhof T.C."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/author | "Missler M."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/author | "Aramuni G."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/author | "Rohlmann A."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/author | "Sargsyan V."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/name | "J Neurosci"xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/pages | "4330-4342"xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/title | "Extracellular domains of alpha-neurexins participate in regulating synaptic transmission by selectively affecting N- and P/Q-type Ca2+ channels."xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://purl.uniprot.org/core/volume | "25"xsd:string |
| http://purl.uniprot.org/citations/15858059 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15858059 |
| http://purl.uniprot.org/citations/15858059 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15858059 |
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| http://purl.uniprot.org/uniprot/#_G3UWQ9-mappedCitation-15858059 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15858059 |