| http://purl.uniprot.org/citations/21228161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21228161 | http://www.w3.org/2000/01/rdf-schema#comment | "Synapse formation requires the organization of presynaptic active zones, the synaptic vesicle release sites, in precise apposition to postsynaptic neurotransmitter receptor clusters; however, the molecular mechanisms responsible for these processes remain unclear. Here, we show that P/Q-type and N-type voltage-dependent calcium channels (VDCCs) play essential roles as scaffolding proteins in the organization of presynaptic active zones. The neuromuscular junction of double knock-out mice for P/Q- and N-type VDCCs displayed a normal size but had significantly reduced numbers of active zones and docked vesicles and featured an attenuation of the active-zone proteins Bassoon, Piccolo, and CAST/Erc2. Consistent with this phenotype, direct interactions of the VDCC β1b or β4 subunits and the active zone-specific proteins Bassoon or CAST/Erc2 were confirmed by immunoprecipitation. A decrease in the number of active zones caused by a loss of presynaptic VDCCs resembled the pathological conditions observed in the autoimmune neuromuscular disorder Lambert-Eaton myasthenic syndrome. At the synaptic cleft of double knock-out mice, we also observed a decrease of the synaptic organizer laminin β2 protein, an extracellular ligand of P/Q- and N-type VDCCs. However, the transcription level of laminin β2 did not decrease in double knock-out mice, suggesting that the synaptic accumulation of laminin β2 protein required its interaction with presynaptic VDCCs. These results suggest that presynaptic VDCCs link the target-derived synapse organizer laminin β2 to active-zone proteins and function as scaffolding proteins to anchor active-zone proteins to the presynaptic membrane."xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.org/dc/terms/identifier | "doi:10.1523/jneurosci.3771-10.2011"xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/author | "Nishimune H."xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/author | "Billings S.E."xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/name | "J Neurosci"xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/pages | "512-525"xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/title | "Calcium channels link the muscle-derived synapse organizer laminin beta2 to Bassoon and CAST/Erc2 to organize presynaptic active zones."xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://purl.uniprot.org/core/volume | "31"xsd:string |
| http://purl.uniprot.org/citations/21228161 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21228161 |
| http://purl.uniprot.org/citations/21228161 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21228161 |
| http://purl.uniprot.org/uniprot/#_A0A0A6YWI2-mappedCitation-21228161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21228161 |
| http://purl.uniprot.org/uniprot/#_A0A0A6YWR0-mappedCitation-21228161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21228161 |
| http://purl.uniprot.org/uniprot/#_A0A0A6YWY6-mappedCitation-21228161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21228161 |
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| http://purl.uniprot.org/uniprot/#_A0A2I3BPY2-mappedCitation-21228161 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21228161 |