| pubmed-article:10944212 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C1156135 | lld:lifeskim |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:10944212 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:10944212 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:10944212 | pubmed:dateCreated | 2000-9-19 | lld:pubmed |
| pubmed-article:10944212 | pubmed:abstractText | Yeast vacuoles undergo priming, docking, and homotypic fusion, although little has been known of the connections between these reactions. Vacuole-associated Vam2p and Vam6p (Vam2/6p) are components of a 65S complex containing SNARE proteins. Upon priming by Sec18p/NSF and ATP, Vam2/6p is released as a 38S subcomplex that binds Ypt7p to initiate docking. We now report that the 38S complex consists of both Vam2/6p and the class C Vps proteins [Reider, S. E. and Emr, S. D. (1997) Mol. Biol. Cell 8, 2307-2327]. This complex includes Vps33p, a member of the Sec1 family of proteins that bind t-SNAREs. We term this 38S complex HOPS, for homotypic fusion and vacuole protein sorting. This unexpected finding explains how Vam2/6p associates with SNAREs and provides a mechanistic link of the class C Vps proteins to Ypt/Rab action. HOPS initially associates with vacuole SNAREs in "cis" and, after release by priming, hops to Ypt7p, activating this Ypt/Rab switch to initiate docking. | lld:pubmed |
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| pubmed-article:10944212 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10944212 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10944212 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10944212 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10944212 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10944212 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10944212 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10944212 | pubmed:author | pubmed-author:PriceAA | lld:pubmed |
| pubmed-article:10944212 | pubmed:author | pubmed-author:WicknerW TWT | lld:pubmed |
| pubmed-article:10944212 | pubmed:author | pubmed-author:MargolisNN | lld:pubmed |
| pubmed-article:10944212 | pubmed:author | pubmed-author:SealsD FDF | lld:pubmed |
| pubmed-article:10944212 | pubmed:author | pubmed-author:EitzenGG | lld:pubmed |
| pubmed-article:10944212 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10944212 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10944212 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10944212 | pubmed:owner | NLM | lld:pubmed |
