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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1998-6-26
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pubmed:databankReference |
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pubmed:abstractText |
Syntaxin-1 is a component of the synaptic vesicle docking and/or membrane fusion soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) complex (7S and 20S complexes) in nerve terminals. Syntaxin-1 also forms a heterodimer with Munc18/n-Sec1/rbSec1 in a complex that is distinct from the 7S and 20S complexes. In this report, we identify a novel syntaxin-1-binding protein, tomosyn, that is capable of dissociating Munc18 from syntaxin-1 and forming a novel 10S complex with syntaxin-1, soluble N-etyhlmaleimide-sensitive factor attachment (SNAP) 25, and synaptotagmin. The 130 kDa isoform of tomosyn is specifically expressed in brain, where its distribution partly overlaps with that of syntaxin-1 in nerve terminals. High level expression of either syntaxin-1 or tomosyn results in a specific reduction in Ca2+-dependent exocytosis from PC12 cells. These results suggest that tomosyn is an important component in the neurotransmitter release process where it may stimulate SNARE complex formation.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Munc18 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotransmitter Agents,
http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Stx1a protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Syntaxin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0896-6273
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pubmed:author |
pubmed-author:AsakuraTT,
pubmed-author:FujitaYY,
pubmed-author:KotaniHH,
pubmed-author:MatsuuraYY,
pubmed-author:MizoguchiAA,
pubmed-author:NishiokaHH,
pubmed-author:OhyaTT,
pubmed-author:SakisakaTT,
pubmed-author:SchellerR HRH,
pubmed-author:ShiratakiHH,
pubmed-author:TakaiYY,
pubmed-author:YokoyamaSS
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
905-15
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9620695-Animals,
pubmed-meshheading:9620695-Antigens, Surface,
pubmed-meshheading:9620695-Blotting, Western,
pubmed-meshheading:9620695-Brain Chemistry,
pubmed-meshheading:9620695-COS Cells,
pubmed-meshheading:9620695-Calcium,
pubmed-meshheading:9620695-Carrier Proteins,
pubmed-meshheading:9620695-Cloning, Molecular,
pubmed-meshheading:9620695-DNA, Complementary,
pubmed-meshheading:9620695-Exocytosis,
pubmed-meshheading:9620695-Isomerism,
pubmed-meshheading:9620695-Molecular Sequence Data,
pubmed-meshheading:9620695-Munc18 Proteins,
pubmed-meshheading:9620695-Nerve Tissue Proteins,
pubmed-meshheading:9620695-Neurons,
pubmed-meshheading:9620695-Neuropeptides,
pubmed-meshheading:9620695-Neurotransmitter Agents,
pubmed-meshheading:9620695-PC12 Cells,
pubmed-meshheading:9620695-Protein Binding,
pubmed-meshheading:9620695-R-SNARE Proteins,
pubmed-meshheading:9620695-Rats,
pubmed-meshheading:9620695-Synaptic Transmission,
pubmed-meshheading:9620695-Syntaxin 1,
pubmed-meshheading:9620695-Vesicular Transport Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process.
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pubmed:affiliation |
Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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