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rdf:type |
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lifeskim:mentions |
umls-concept:C0030685,
umls-concept:C0169268,
umls-concept:C0332466,
umls-concept:C0391871,
umls-concept:C0441471,
umls-concept:C0680255,
umls-concept:C0752065,
umls-concept:C0851285,
umls-concept:C1283071,
umls-concept:C1522240,
umls-concept:C1522290,
umls-concept:C1963578
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pubmed:issue |
3
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pubmed:dateCreated |
1998-2-12
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pubmed:abstractText |
The N-ethylmaleimide-sensitive factor (NSF) is required for multiple intracellular vesicle transport events. In vitro biochemical studies have demonstrated that NSF, soluble NSF attachment proteins (SNAPs), and SNAP receptors from a 20 S particle. This complex is disassembled by the ATPase activity of NSF. We have studied particle disassembly in a membrane environment by examining the binding of recombinant SNAPs and NSF to endosomal membranes. We present evidence that alpha-SNAP is released from the membranes in a temperature- and time-dependent manner and that this release is mediated by the ATPase activity of NSF. Our results indicate that NSF mutants in the first ATP binding domain completely abrogate alpha-SNAP release, whereas no inhibitory effect is observed with a mutant in the second ATP binding domain. Interestingly, neither beta-SNAP nor gamma-SNAP are released by the ATPase activity of NSF, indicating that these proteins are retained on the membranes by interactions that differ from those that retain alpha-SNAP. Although the small Rab GTPases are known to play a role in SNARE complex assembly, our results indicate that these GTPases do not regulate the NSF-dependent release of alpha-SNAP.
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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 Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GDP dissociation inhibitor 1,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Dissociation...,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Ethylmaleimide-Sensitive Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Soluble N-Ethylmaleimide-Sensitive...,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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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 |
16
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1334-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9430666-Adenosine Triphosphatases,
pubmed-meshheading:9430666-Adenosine Triphosphate,
pubmed-meshheading:9430666-Animals,
pubmed-meshheading:9430666-Binding Sites,
pubmed-meshheading:9430666-Carrier Proteins,
pubmed-meshheading:9430666-Cell Membrane,
pubmed-meshheading:9430666-GTP Phosphohydrolases,
pubmed-meshheading:9430666-GTP-Binding Proteins,
pubmed-meshheading:9430666-Guanine Nucleotide Dissociation Inhibitors,
pubmed-meshheading:9430666-Hydrolysis,
pubmed-meshheading:9430666-Membrane Proteins,
pubmed-meshheading:9430666-N-Ethylmaleimide-Sensitive Proteins,
pubmed-meshheading:9430666-Soluble N-Ethylmaleimide-Sensitive Factor Attachment...,
pubmed-meshheading:9430666-Temperature,
pubmed-meshheading:9430666-Vesicular Transport Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
N-ethylmaleimide-sensitive factor-dependent alpha-SNAP release, an early event in the docking/fusion process, is not regulated by Rab GTPases.
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pubmed:affiliation |
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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