| pubmed-article:18268324 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18268324 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:18268324 | lifeskim:mentions | umls-concept:C1622418 | lld:lifeskim |
| pubmed-article:18268324 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:18268324 | lifeskim:mentions | umls-concept:C0017547 | lld:lifeskim |
| pubmed-article:18268324 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:18268324 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:18268324 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:18268324 | pubmed:dateCreated | 2008-2-21 | lld:pubmed |
| pubmed-article:18268324 | pubmed:abstractText | Exocytic vesicle fusion requires both the SNARE family of fusion proteins and a closely associated regulatory subunit of the Sec1/Munc18 (SM) family. In principle, SM proteins could act at an early SNARE assembly step to promote vesicle-plasma membrane adhesion or at a late step to overcome the energetic barrier for fusion. Here, we use the neuronal cognates of each of these protein families to recapitulate, and distinguish, membrane adhesion and fusion on a novel lipidic platform suitable for imaging by fluorescence microscopy. Vesicle SNARE (v-SNARE) proteins reconstituted into giant vesicles ( approximately 10 mum) are fully mobile and functional. Through confocal microscopy, we observe that large vesicles ( approximately 100 nm) carrying target membrane SNAREs (t-SNAREs) both adhere to and freely move on the surface of the v-SNARE giant vesicle. Under conditions where the intrinsic ability of SNAREs to drive fusion is minimized, Munc18 stimulates both SNARE-dependent stable adhesion and fusion. Furthermore, mutation of a critical Munc18-binding residue on the N terminus of the t-SNARE syntaxin uncouples Munc18-stimulated vesicle adhesion from membrane fusion. We expect that the study of SNARE-mediated fusion with giant membranes will find wide applicability in distinguishing adhesion- and fusion-directed SNARE regulatory factors. | lld:pubmed |
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| pubmed-article:18268324 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18268324 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18268324 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18268324 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18268324 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18268324 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:18268324 | pubmed:author | pubmed-author:ShenJingshiJ | lld:pubmed |
| pubmed-article:18268324 | pubmed:author | pubmed-author:RothmanJames... | lld:pubmed |
| pubmed-article:18268324 | pubmed:author | pubmed-author:MeliaThomas... | lld:pubmed |
| pubmed-article:18268324 | pubmed:author | pubmed-author:TaresteDavidD | lld:pubmed |
| pubmed-article:18268324 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18268324 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:18268324 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:18268324 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18268324 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18268324 | pubmed:pagination | 2380-5 | lld:pubmed |
| pubmed-article:18268324 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:18268324 | pubmed:meshHeading | pubmed-meshheading:18268324... | lld:pubmed |
| pubmed-article:18268324 | pubmed:meshHeading | pubmed-meshheading:18268324... | lld:pubmed |
| pubmed-article:18268324 | pubmed:meshHeading | pubmed-meshheading:18268324... | lld:pubmed |
| pubmed-article:18268324 | pubmed:meshHeading | pubmed-meshheading:18268324... | lld:pubmed |
| pubmed-article:18268324 | pubmed:meshHeading | pubmed-meshheading:18268324... | lld:pubmed |
| pubmed-article:18268324 | pubmed:meshHeading | pubmed-meshheading:18268324... | lld:pubmed |
| pubmed-article:18268324 | pubmed:meshHeading | pubmed-meshheading:18268324... | lld:pubmed |
| pubmed-article:18268324 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18268324 | pubmed:articleTitle | SNAREpin/Munc18 promotes adhesion and fusion of large vesicles to giant membranes. | lld:pubmed |
| pubmed-article:18268324 | pubmed:affiliation | Department of Physiology and Cellular Biophysics, Columbia University, 1150 St. Nicholas Avenue, New York, NY 10032, USA. | lld:pubmed |
| pubmed-article:18268324 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18268324 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18268324 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18268324 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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