| pubmed-article:20603329 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C0009498 | lld:lifeskim |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C0025246 | lld:lifeskim |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C0288881 | lld:lifeskim |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C0300824 | lld:lifeskim |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C0547040 | lld:lifeskim |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C1420506 | lld:lifeskim |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C0183362 | lld:lifeskim |
| pubmed-article:20603329 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:20603329 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:20603329 | pubmed:dateCreated | 2010-7-13 | lld:pubmed |
| pubmed-article:20603329 | pubmed:abstractText | Sec1/Munc18 (SM) proteins activate intracellular membrane fusion through binding to cognate SNAP receptor (SNARE) complexes. The synaptic target membrane SNARE syntaxin 1 contains a highly conserved H(abc) domain, which connects an N-peptide motif to the SNARE core domain and is thought to participate in the binding of Munc18-1 (the neuronal SM protein) to the SNARE complex. Unexpectedly, we found that mutation or complete removal of the H(abc) domain had no effect on Munc18-1 stimulation of fusion. The central cavity region of Munc18-1 is required to stimulate fusion but not through its binding to the syntaxin H(abc) domain. SNAP-25, another synaptic SNARE subunit, contains a flexible linker and exhibits an atypical conjoined Q(bc) configuration. We found that neither the linker nor the Q(bc) configuration is necessary for Munc18-1 promotion of fusion. As a result, Munc18-1 activates a SNARE complex with the typical configuration, in which each of the SNARE core domains is individually rooted in the membrane bilayer. Thus, the SNARE four-helix bundle and syntaxin N-peptide constitute a minimal complement for Munc18-1 activation of fusion. | lld:pubmed |
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| pubmed-article:20603329 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20603329 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20603329 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20603329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20603329 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20603329 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:20603329 | pubmed:issn | 1540-8140 | lld:pubmed |
| pubmed-article:20603329 | pubmed:author | pubmed-author:ShenJingshiJ | lld:pubmed |
| pubmed-article:20603329 | pubmed:author | pubmed-author:RothmanJames... | lld:pubmed |
| pubmed-article:20603329 | pubmed:author | pubmed-author:RathoreShaile... | lld:pubmed |
| pubmed-article:20603329 | pubmed:author | pubmed-author:KhandanLavanL | lld:pubmed |
| pubmed-article:20603329 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20603329 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:20603329 | pubmed:volume | 190 | lld:pubmed |
