| pubmed-article:7835333 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7835333 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:7835333 | lifeskim:mentions | umls-concept:C0085255 | lld:lifeskim |
| pubmed-article:7835333 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:7835333 | lifeskim:mentions | umls-concept:C0078208 | lld:lifeskim |
| pubmed-article:7835333 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:7835333 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
| pubmed-article:7835333 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:7835333 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7835333 | pubmed:dateCreated | 1995-2-27 | lld:pubmed |
| pubmed-article:7835333 | pubmed:abstractText | The synaptic vesicle protein synaptobrevin (VAMP) has recently been implicated as one of the key proteins involved in exocytotic membrane fusion. It interacts with the synaptic membrane proteins syntaxin I and synaptosome-associated protein (SNAP)-25 to form a complex which precedes exocytosis [Söllner et al. (1993b) Cell, 75, 409-418]. Here we demonstrate that the majority of synaptobrevin is bound to the vesicle protein synaptophysin in detergent extracts. No syntaxin I was found in this complex when synaptophysin-specific antibodies were used for immunoprecipitation. Conversely, no synaptophysin was associated with the synaptobrevin-syntaxin I complex when syntaxin-specific antibodies were used for immunoprecipitation. Thus, the synaptobrevin pool bound to synaptophysin is not available for binding to syntaxin I and SNAP-25, and vice versa. Synaptobrevin-synaptophysin binding was also demonstrated by chemical cross-linking in isolated nerve terminals. Furthermore, recombinant synaptobrevin II efficiently bound synaptophysin and its isoform synaptoporin, but not the more distantly related synaptic vesicle protein p29. Recombinant synaptobrevin I bound with similar efficiency, whereas the non-neuronal isoform cellubrevin displayed a lower affinity towards synaptophysin. Treatment with high NaCl concentrations resulted in a dissociation of the synaptobrevin-synaptophysin complex. In addition, the interaction of synaptobrevin with synaptophysin was irreversibly abolished by low amounts of SDS, while the interaction with syntaxin I was enhanced. We conclude that synaptophysin selectively interacts with synaptobrevin in a complex which excludes the t-SNAP receptors syntaxin I and SNAP-25, suggesting a role for synaptophysin in the control of exocytosis. | lld:pubmed |
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| pubmed-article:7835333 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7835333 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7835333 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7835333 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7835333 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7835333 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7835333 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:7835333 | pubmed:author | pubmed-author:ChartonLL | lld:pubmed |
| pubmed-article:7835333 | pubmed:author | pubmed-author:EdelmannLL | lld:pubmed |
| pubmed-article:7835333 | pubmed:author | pubmed-author:JahnRR | lld:pubmed |
| pubmed-article:7835333 | pubmed:author | pubmed-author:HansonP IPI | lld:pubmed |
| pubmed-article:7835333 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7835333 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:7835333 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:7835333 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7835333 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7835333 | pubmed:pagination | 224-31 | lld:pubmed |
| pubmed-article:7835333 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:7835333 | pubmed:meshHeading | pubmed-meshheading:7835333-... | lld:pubmed |
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| pubmed-article:7835333 | pubmed:meshHeading | pubmed-meshheading:7835333-... | lld:pubmed |
| pubmed-article:7835333 | pubmed:meshHeading | pubmed-meshheading:7835333-... | lld:pubmed |
| pubmed-article:7835333 | pubmed:meshHeading | pubmed-meshheading:7835333-... | lld:pubmed |
| pubmed-article:7835333 | pubmed:meshHeading | pubmed-meshheading:7835333-... | lld:pubmed |
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| pubmed-article:7835333 | pubmed:meshHeading | pubmed-meshheading:7835333-... | lld:pubmed |
| pubmed-article:7835333 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7835333 | pubmed:articleTitle | Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. | lld:pubmed |
