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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
1995-11-14
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pubmed:abstractText |
While there is compelling evidence that the synaptic vesicle protein synaptotagmin serves as the major Ca2+ sensor for regulated exocytosis, it is not known how Ca2+ binding initiates membrane fusion. Here we report that Ca2+ increases the affinity, by approximately 2 orders of magnitude, between synaptotagmin and syntaxin 1, a component of the synaptic fusion apparatus. This effect is specific for divalent cations which can stimulate exocytosis of synaptic vesicles (Ca2+ > Ba2+, Sr2+ >> Mg2+). The Ca(2+)-dependence of the interaction was composed of two components with EC50 values of 0.7 and 180 microM Ca2+. The interaction is mediated by the carboxyl-terminal region of syntaxin 1 (residues 194-288) and is regulated by a novel Ca(2+)-binding site(s) which does not require phospholipids and is not disrupted by mutations that abolish Ca(2+)-dependent phospholipid binding to synaptotagmin. We propose that this interaction constitutes an essential step in excitation-secretion coupling.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Stx1a protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins,
http://linkedlifedata.com/resource/pubmed/chemical/Syntaxin 1
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23667-71
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7559535-Amino Acid Sequence,
pubmed-meshheading:7559535-Animals,
pubmed-meshheading:7559535-Antigens, Surface,
pubmed-meshheading:7559535-Binding Sites,
pubmed-meshheading:7559535-Brain,
pubmed-meshheading:7559535-Calcium,
pubmed-meshheading:7559535-Calcium-Binding Proteins,
pubmed-meshheading:7559535-Exocytosis,
pubmed-meshheading:7559535-Membrane Glycoproteins,
pubmed-meshheading:7559535-Molecular Sequence Data,
pubmed-meshheading:7559535-Molecular Structure,
pubmed-meshheading:7559535-Nerve Tissue Proteins,
pubmed-meshheading:7559535-Protein Binding,
pubmed-meshheading:7559535-Protein Conformation,
pubmed-meshheading:7559535-Rats,
pubmed-meshheading:7559535-Recombinant Proteins,
pubmed-meshheading:7559535-Sequence Deletion,
pubmed-meshheading:7559535-Synaptic Vesicles,
pubmed-meshheading:7559535-Synaptotagmins,
pubmed-meshheading:7559535-Syntaxin 1
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pubmed:year |
1995
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pubmed:articleTitle |
Ca2+ regulates the interaction between synaptotagmin and syntaxin 1.
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pubmed:affiliation |
Howard Hughes Medical Institute, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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