Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2005-4-11
pubmed:abstractText
Yeast vacuole fusion requires palmitoylated Vac8. We previously showed that Vac8 acylation occurs early in the fusion reaction, is blocked by antibodies against Sec18 (yeast N-ethylmaleimide-sensitive fusion protein (NSF)), and is mediated by the R-SNARE Ykt6. Here we analyzed the regulation of this reaction on purified vacuoles. We show that Vac8 acylation is restricted to a narrow time window, is independent of ATP hydrolysis by Sec18, and is stimulated by the ion chelator EDTA. Analysis of vacuole protein complexes indicated that Ykt6 is part of a complex distinct from the second R-SNARE, Nyv1. We speculate that during vacuole fusion, Nyv1 is the classical R-SNARE, whereas the Ykt6-containing complex has a novel function in Vac8 palmitoylation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid, http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SEC18 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/VAC8 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/YKT6 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15348-55
pubmed:dateRevised
2009-7-1
pubmed:meshHeading
pubmed-meshheading:15701652-Adenosine Triphosphatases, pubmed-meshheading:15701652-Adenosine Triphosphate, pubmed-meshheading:15701652-Dose-Response Relationship, Drug, pubmed-meshheading:15701652-Edetic Acid, pubmed-meshheading:15701652-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15701652-Genotype, pubmed-meshheading:15701652-Glutathione Transferase, pubmed-meshheading:15701652-Hydrolysis, pubmed-meshheading:15701652-Immunoprecipitation, pubmed-meshheading:15701652-Lipoproteins, pubmed-meshheading:15701652-Membrane Proteins, pubmed-meshheading:15701652-Microscopy, Phase-Contrast, pubmed-meshheading:15701652-Models, Biological, pubmed-meshheading:15701652-Palmitic Acid, pubmed-meshheading:15701652-Protein Binding, pubmed-meshheading:15701652-R-SNARE Proteins, pubmed-meshheading:15701652-Recombinant Proteins, pubmed-meshheading:15701652-SNARE Proteins, pubmed-meshheading:15701652-Saccharomyces cerevisiae, pubmed-meshheading:15701652-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15701652-Time Factors, pubmed-meshheading:15701652-Vacuoles, pubmed-meshheading:15701652-Vesicular Transport Proteins
pubmed:year
2005
pubmed:articleTitle
ATP-independent control of Vac8 palmitoylation by a SNARE subcomplex on yeast vacuoles.
pubmed:affiliation
Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't