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http://purl.uniprot.org/citations/9162066http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9162066http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9162066http://www.w3.org/2000/01/rdf-schema#comment"Synaptotagmin I is a Ca2+-binding protein of synaptic vesicles that serves as a Ca2+ sensor for neurotransmitter release and was the first member found of a large family of trafficking proteins. We have now identified a novel synaptotagmin, synaptotagmin XI, that is highly expressed in brain and at lower levels in other tissues. Like other synaptotagmins, synaptotagmin XI has a single transmembrane region and two cytoplasmic C2-domains but is most closely related to synaptotagmin IV with which it forms a new subclass of synaptotagmins. The first C2-domain of synaptotagmin I (the C2A-domain) binds phospholipids as a function of Ca2+ and contains a Ca2+-binding site, the C2-motif, that binds at least two Ca2+ ions via five aspartate residues and is conserved in most C2-domains (Shao, X., Davletov, B., Sutton, B., Südhof, T. C., Rizo, J. R. (1996) Science 273, 248-253). In the C2A-domains of synaptotagmins IV and XI, however, one of the five Ca2+-binding aspartates in the C2-motif is substituted for a serine, suggesting that these C2-domains do not bind Ca2+. To test this, we produced recombinant C2A-domains from synaptotagmins IV and XI with either wild type serine or mutant aspartate in the C2-motif. Circular dichroism showed that Ca2+ stabilizes both mutant but not wild type C2-domains against temperature-induced denaturation, indicating that the mutations restore Ca2+-binding to the wild type C2-domains. Furthermore, wild type C2A-domains of synaptotagmins IV and XI exhibited no Ca2+-dependent phospholipid binding, whereas mutant C2A-domains bound phospholipids as a function of Ca2+ similarly to wild type synaptotagmin I. These experiments suggest that a class of synaptotagmins was selected during evolution in which the Ca2+-binding site of the C2A-domain was inactivated by a single point mutation. Thus, synaptotagmins must have Ca2+-independent functions as well as Ca2+-dependent functions that are selectively maintained in distinct members of this gene family."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.22.14314"xsd:string
http://purl.uniprot.org/citations/9162066http://purl.org/dc/terms/identifier"doi:10.1074/jbc.272.22.14314"xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Suedhof T.C."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Suedhof T.C."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Shao X."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Shao X."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Ichtchenko K."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Ichtchenko K."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Rizo J."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"Rizo J."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"von Poser C."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/author"von Poser C."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/pages"14314-14319"xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/pages"14314-14319"xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/title"The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/title"The evolutionary pressure to inactivate. A subclass of synaptotagmins with an amino acid substitution that abolishes Ca2+ binding."xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/volume"272"xsd:string
http://purl.uniprot.org/citations/9162066http://purl.uniprot.org/core/volume"272"xsd:string
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