Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6453
pubmed:dateCreated
1993-12-30
pubmed:databankReference
pubmed:abstractText
Three synaptic proteins, syntaxin, SNAP-25 and synaptobrevin, were recently identified as targets of clostridial neurotoxins that irreversibly inhibit synaptic vesicle fusion. Experiments searching for membrane receptors for N-ethylmaleimide-sensitive fusion protein (NSF), which has an important role in membrane fusion, revealed an ATP-dependent interaction of the same three synaptic proteins with NSF and its soluble attachment proteins. Thus, two independent approaches identify syntaxin, synaptobrevin and SNAP-25 as components of the synaptic vesicle fusion machinery, but their mode of action is unclear. We have now discovered a brain protein of relative molecular mass 67,000 (67K) which binds stably to syntaxin. Amino-acid sequencing and complementary DNA cloning revealed that the 67K protein is encoded by the mammalian homologue of the Caenorhabditis elegans gene unc-18. In C. elegans, unc-18 belongs to a group of genes defined by mutations with a paralytic phenotype and accumulations of acetylcholine, suggesting a defect in neurotransmitter release. The binding of the mammalian homologue of unc-18 (Munc-18) to syntaxin requires the N terminus of syntaxin whereas that of SNAP-25 involves a more C-terminal sequence. Our data suggest that Munc-18 is a previously unidentified essential component of the synaptic vesicle fusion protein complex.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Munc18 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Syntaxin 1, http://linkedlifedata.com/resource/pubmed/chemical/Unc-18 protein, C elegans, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
366
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
347-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:8247129-Amino Acid Sequence, pubmed-meshheading:8247129-Animals, pubmed-meshheading:8247129-Antigens, Surface, pubmed-meshheading:8247129-Base Sequence, pubmed-meshheading:8247129-Brain Chemistry, pubmed-meshheading:8247129-Caenorhabditis elegans, pubmed-meshheading:8247129-Caenorhabditis elegans Proteins, pubmed-meshheading:8247129-Carrier Proteins, pubmed-meshheading:8247129-Cattle, pubmed-meshheading:8247129-Helminth Proteins, pubmed-meshheading:8247129-Membrane Fusion, pubmed-meshheading:8247129-Molecular Sequence Data, pubmed-meshheading:8247129-Munc18 Proteins, pubmed-meshheading:8247129-Nerve Tissue Proteins, pubmed-meshheading:8247129-Phosphoproteins, pubmed-meshheading:8247129-Protein Binding, pubmed-meshheading:8247129-Rats, pubmed-meshheading:8247129-Recombinant Fusion Proteins, pubmed-meshheading:8247129-Sequence Homology, Amino Acid, pubmed-meshheading:8247129-Synaptic Vesicles, pubmed-meshheading:8247129-Syntaxin 1, pubmed-meshheading:8247129-Vesicular Transport Proteins
pubmed:year
1993
pubmed:articleTitle
Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin.
pubmed:affiliation
Howard Hughes Medical Institute, University of Texas Southwestern Medical School, Dallas 75235.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't