Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-8-1
pubmed:abstractText
N-ethylmaleimide-sensitive fusion protein (NSF) and its co-factor soluble NSF attachment protein (alpha)-SNAP) are essential components of the synaptic vesicle fusion machinery and form part of a structurally-conserved 20S protein complex. However, their precise function, relative to fusion itself, is not clear. Using a UV-activated cross-linking approach, we have measured the rate at which a single round of NSF-driven ATP hydrolysis leads to 20S complex disassembly within synaptic membranes. Although this rate is substantially faster than previous estimates of NSF-dependent ATP hydrolysis, it remains much lower than published rates for fusion of synaptic vesicles. Furthermore, the stability of 20S complexes is unaffected by Ca(2+) at concentrations that elicit rapid membrane fusion. We conclude that the ATPase activity of NSF does not contribute directly to vesicle fusion, but more likely plays an earlier role in the synaptic vesicle cycle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
113 ( Pt 10)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1783-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10769209-Animals, pubmed-meshheading:10769209-Calcium, pubmed-meshheading:10769209-Carrier Proteins, pubmed-meshheading:10769209-Cell Extracts, pubmed-meshheading:10769209-Cross-Linking Reagents, pubmed-meshheading:10769209-Exocytosis, pubmed-meshheading:10769209-Kinetics, pubmed-meshheading:10769209-Magnesium, pubmed-meshheading:10769209-Membrane Fusion, pubmed-meshheading:10769209-Membrane Proteins, pubmed-meshheading:10769209-N-Ethylmaleimide-Sensitive Proteins, pubmed-meshheading:10769209-SNARE Proteins, pubmed-meshheading:10769209-Soluble N-Ethylmaleimide-Sensitive Factor Attachment..., pubmed-meshheading:10769209-Swine, pubmed-meshheading:10769209-Synaptic Membranes, pubmed-meshheading:10769209-Synaptic Vesicles, pubmed-meshheading:10769209-Time Factors, pubmed-meshheading:10769209-Ultraviolet Rays, pubmed-meshheading:10769209-Vesicular Transport Proteins
pubmed:year
2000
pubmed:articleTitle
Disassembly of membrane-associated NSF 20S complexes is slow relative to vesicle fusion and is Ca(2+)-independent.
pubmed:affiliation
Division of Biochemistry, School of Biological Sciences, University of Manchester, Oxford Road, Manchester, M13 9PT, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't