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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-8-13
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pubmed:abstractText |
Biochemical studies suggest that syntaxin 1A participates in multiple protein-protein interactions in the synaptic terminal, but the in vivo significance of these interactions is poorly understood. We used a targeted mutagenesis approach to eliminate specific syntaxin binding interactions and demonstrate that Drosophila syntaxin 1A plays multiple regulatory roles in neurotransmission in vivo. Syntaxin mutations that eliminate ROP/Munc-18 binding display increased neurotransmitter release, suggesting that ROP inhibits neurosecretion through its interaction with syntaxin. Syntaxin mutations that block Ca2+ channel binding also cause an increase in neurotransmitter release, suggesting that syntaxin normally functions in inhibiting Ca2+ channel opening. Additionally, we identify and characterize a syntaxin Ca2+ effector domain, which may spatially organize the Ca2+ channel, cysteine string protein, and synaptotagmin for effective excitation-secretion coupling in the presynaptic terminal.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:keyword |
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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/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Munc18 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotransmitter Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Rop protein, Drosophila,
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 |
Jul
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
593-605
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10433270-Animals,
pubmed-meshheading:10433270-Animals, Genetically Modified,
pubmed-meshheading:10433270-Antigens, Surface,
pubmed-meshheading:10433270-Binding, Competitive,
pubmed-meshheading:10433270-Calcium,
pubmed-meshheading:10433270-Drosophila,
pubmed-meshheading:10433270-Drosophila Proteins,
pubmed-meshheading:10433270-Electrophysiology,
pubmed-meshheading:10433270-Exocytosis,
pubmed-meshheading:10433270-Munc18 Proteins,
pubmed-meshheading:10433270-Muscle Contraction,
pubmed-meshheading:10433270-Mutagenesis, Site-Directed,
pubmed-meshheading:10433270-Nerve Tissue Proteins,
pubmed-meshheading:10433270-Neurotransmitter Agents,
pubmed-meshheading:10433270-Protein Structure, Tertiary,
pubmed-meshheading:10433270-Synaptic Transmission,
pubmed-meshheading:10433270-Synaptic Vesicles,
pubmed-meshheading:10433270-Syntaxin 1,
pubmed-meshheading:10433270-Vesicular Transport Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Syntaxin 1A interacts with multiple exocytic proteins to regulate neurotransmitter release in vivo.
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pubmed:affiliation |
Department of Cell Biology, Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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