| http://purl.uniprot.org/citations/10397765 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10397765 | http://www.w3.org/2000/01/rdf-schema#comment | "Synaptotagmins (Syts) are a family of vesicle proteins that have been implicated in both regulated neurosecretion and general membrane trafficking. Calcium-dependent interactions mediated through their C2 domains are proposed to contribute to the mechanism by which Syts trigger calcium-dependent neurotransmitter release. Syt IV is a novel member of the Syt family that is induced by cell depolarization and has a rapid rate of synthesis and a short half-life. Moreover, the C2A domain of Syt IV does not bind calcium. We have examined the biochemical and functional properties of the C2 domains of Syt IV. Consistent with its non-calcium binding properties, the C2A domain of Syt IV binds syntaxin isoforms in a calcium-independent manner. In neuroendocrine pheochromocytoma (PC12) cells, Syt IV colocalizes with Syt I in the tips of the neurites. Microinjection of the C2A domain reveals that calcium-independent interactions mediated through this domain of Syt IV inhibit calcium-mediated neurotransmitter release from PC12 cells. Conversely, the C2B domain of Syt IV contains calcium binding properties, which permit homo-oligomerization as well as hetero-oligomerization with Syt I. Our observation that different combinatorial interactions exist between Syt and syntaxin isoforms, coupled with the calcium stimulated hetero-oligomerization of Syt isoforms, suggests that the secretory machinery contains a vast repertoire of biochemical properties for sensing calcium and regulating neurotransmitter release accordingly."xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.10.7.2285"xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/author | "Herschman H.R."xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/author | "Elferink L.A."xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/author | "Ferguson G.D."xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/author | "Thomas D.M."xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/name | "Mol Biol Cell"xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/pages | "2285-2295"xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/title | "Functional and biochemical analysis of the C2 domains of synaptotagmin IV."xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://purl.uniprot.org/core/volume | "10"xsd:string |
| http://purl.uniprot.org/citations/10397765 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10397765 |
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