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http://purl.uniprot.org/citations/23401610http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23401610http://www.w3.org/2000/01/rdf-schema#comment"Complexins (Cplxs) are small, SNARE-associated proteins believed to regulate fast, calcium-triggered exocytosis. However, studies have pointed to either an inhibitory and/or facilitatory role in exocytosis, and the role of Cplxs in synchronizing exocytosis is relatively unexplored. Here, we compare the function of two types of complexin, Cplx 1 and 2, in two model systems of calcium-dependent exocytosis. In mouse neuromuscular junctions (NMJs), we find that lack of Cplx 1 significantly reduces and desynchronizes calcium-triggered synaptic transmission; furthermore, high-frequency stimulation elicits synaptic facilitation, instead of normal synaptic depression, and the degree of facilitation is highly sensitive to the amount of cytoplasmic calcium buffering. In Cplx 2-null adrenal chromaffin cells, we also find decreased and desynchronized evoked release, and identify a significant reduction in the vesicle pool close to the calcium channels (immediately releasable pool, IRP). Viral transduction with either Cplx 1 or 2 rescues both the size of the evoked response and the synchronicity of release, and it restores the IRP size. Our findings in two model systems are mutually compatible and indicate a role of Cplx 1 and 2 in facilitating vesicle priming, and also lead to the new hypothesis that Cplxs may synchronize vesicle release by promoting coupling between secretory vesicles and calcium channels."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.org/dc/terms/identifier"doi:10.1113/jphysiol.2012.244517"xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/author"Cai H."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/author"Lin M.Y."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/author"Reim K."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/author"Chow R.H."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/author"Ko C.P."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/author"Rohan J.G."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/name"J Physiol"xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/pages"2463-2473"xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/title"Complexin facilitates exocytosis and synchronizes vesicle release in two secretory model systems."xsd:string
http://purl.uniprot.org/citations/23401610http://purl.uniprot.org/core/volume"591"xsd:string
http://purl.uniprot.org/citations/23401610http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23401610
http://purl.uniprot.org/citations/23401610http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23401610
http://purl.uniprot.org/uniprot/#_D3YZ72-mappedCitation-23401610http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23401610
http://purl.uniprot.org/uniprot/#_P63040-mappedCitation-23401610http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23401610
http://purl.uniprot.org/uniprot/#_P84086-mappedCitation-23401610http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23401610
http://purl.uniprot.org/uniprot/P63040http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23401610
http://purl.uniprot.org/uniprot/D3YZ72http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23401610
http://purl.uniprot.org/uniprot/P84086http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23401610