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rdf:type |
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lifeskim:mentions |
umls-concept:C0006675,
umls-concept:C0033684,
umls-concept:C0144255,
umls-concept:C0183210,
umls-concept:C0439851,
umls-concept:C0752274,
umls-concept:C1511625,
umls-concept:C1552596,
umls-concept:C1704675,
umls-concept:C1711351,
umls-concept:C1947931
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pubmed:issue |
15
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pubmed:dateCreated |
1997-10-15
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pubmed:abstractText |
Synaptotagmins are synaptic vesicle proteins containing two calcium-binding C2 domains which are involved in coupling calcium influx through voltage-gated channels to vesicle fusion and exocytosis of neurotransmitters. The interaction of synaptotagmins with native P/Q-type calcium channels was studied in solubilized synaptosomes from rat cerebellum. Antibodies against synaptotagmins I and II, but not IV co-immunoprecipitated [125I]omega-conotoxin MVIIC-labelled calcium channels. Direct interactions were studied between in vitro-translated [35S]synaptotagmin I and fusion proteins containing cytoplasmic loops of the alpha1A subunit (BI isoform). Gel overlay revealed the association of synaptotagmin I with a single region (residues 780-969) located in the intracellular loop connecting homologous domains II and III. Saturable calcium-independent binding occurred with equilibrium dissociation constants of 70 nM and 340 nM at 4 degrees C and pH 7.4, and association was blocked by addition of excess recombinant synaptotagmin I. Direct synaptotagmin binding to the pore-forming subunit of the P/Q-type channel may optimally locate the calcium-binding sites that initiate exocytosis within a zone of voltage-gated calcium entry.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-1334074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-1352065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-1655160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-1718988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-1849233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-6261850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7592870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7623121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7698322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7707358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7778189,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7791877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7832825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7890025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7892240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7901765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7954835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7969483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7971978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-7993622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8097867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8119979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8422678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8524397,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8621455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8636067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8692999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8816702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9303303-8833442
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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/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Cacna1a protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
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 Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmin I,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmin II,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins,
http://linkedlifedata.com/resource/pubmed/chemical/Syt1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Syt2 protein, rat
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4591-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9303303-Amino Acid Sequence,
pubmed-meshheading:9303303-Animals,
pubmed-meshheading:9303303-Antibodies,
pubmed-meshheading:9303303-Binding Sites,
pubmed-meshheading:9303303-Calcium Channels,
pubmed-meshheading:9303303-Calcium-Binding Proteins,
pubmed-meshheading:9303303-Cerebellum,
pubmed-meshheading:9303303-Kinetics,
pubmed-meshheading:9303303-Membrane Glycoproteins,
pubmed-meshheading:9303303-Molecular Sequence Data,
pubmed-meshheading:9303303-Nerve Tissue Proteins,
pubmed-meshheading:9303303-Protein Conformation,
pubmed-meshheading:9303303-Rats,
pubmed-meshheading:9303303-Recombinant Fusion Proteins,
pubmed-meshheading:9303303-Synaptosomes,
pubmed-meshheading:9303303-Synaptotagmin I,
pubmed-meshheading:9303303-Synaptotagmin II,
pubmed-meshheading:9303303-Synaptotagmins
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pubmed:year |
1997
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pubmed:articleTitle |
Direct interaction of the calcium sensor protein synaptotagmin I with a cytoplasmic domain of the alpha1A subunit of the P/Q-type calcium channel.
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pubmed:affiliation |
Institut National de la Sant'e et de la Recherche M'edicale, Unit'e 464, Institut Jean Roche, Facult'e de M'edecine Secteur Nord, Marseille, France.
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