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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1998-10-28
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pubmed:abstractText |
N-Ethylmaleimide-sensitive factor (NSF) plays a key role in vesicular traffic by disassembling and priming SNARE proteins for their function in docking and fusion. We demonstrate that the ATPase activity of NSF is activated by alpha-soluble NSF attachment protein (alpha-SNAP) in a complex with syntaxin 1A. In addition, we show that a construct consisting of the H3 domain of syntaxin IA (GST-synt(195-263), which does not support NSF disassembly in the presence of MgATP gave a larger stimulation. NSF ATPase activation was specific and did not occur using mutant alpha-SNAPs unable to bind GST-synt or with mutated C-termini. We suggest that activation of NSF ATPase activity in the SNARE complex may be essential to allow SNARE priming.
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pubmed:grant |
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Ethylmaleimide-Sensitive Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Soluble N-Ethylmaleimide-Sensitive...,
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 |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
436
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-5
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:9771883-Adenosine Triphosphate,
pubmed-meshheading:9771883-Antigens, Surface,
pubmed-meshheading:9771883-Carrier Proteins,
pubmed-meshheading:9771883-Glutathione Transferase,
pubmed-meshheading:9771883-Hydrolysis,
pubmed-meshheading:9771883-Membrane Proteins,
pubmed-meshheading:9771883-Mutation,
pubmed-meshheading:9771883-N-Ethylmaleimide-Sensitive Proteins,
pubmed-meshheading:9771883-Nerve Tissue Proteins,
pubmed-meshheading:9771883-Recombinant Fusion Proteins,
pubmed-meshheading:9771883-SNARE Proteins,
pubmed-meshheading:9771883-Soluble N-Ethylmaleimide-Sensitive Factor Attachment...,
pubmed-meshheading:9771883-Syntaxin 1,
pubmed-meshheading:9771883-Vesicular Transport Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Stimulation of NSF ATPase activity during t-SNARE priming.
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pubmed:affiliation |
The Physiological Laboratory, University of Liverpool, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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