Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1998-7-27
pubmed:abstractText
Vacuole fusion requires Sec18p (NSF), Sec17p (alpha-SNAP), Ypt7p (GTP binding protein), Vam3p (t-SNARE), Nyv1p (v-SNARE), and LMA1 (low Mr activity 1, a heterodimer of thioredoxin and I(B)2). LMA1 requires Sec18p for saturable, high-affinity binding to vacuoles, and Sec18p "priming" ATPase requires both Sec17p and LMA1. Either the sec18-1 mutation and deletion of I(B)2, or deletion of both I(B)2 and p13 (an I(B)2 homolog) causes a striking synthetic vacuole fragmentation phenotype. Upon Sec18p ATP hydrolysis, LMA1 transfers to (and stabilizes) a Vam3p complex. LMA1 is released from vacuoles in a phosphatase-regulated reaction. This LMA1 cycle explains how priming by Sec18p is coupled to t-SNARE stabilization and to fusion.
pubmed:grant
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/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Microcystins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SEC18 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxins, http://linkedlifedata.com/resource/pubmed/chemical/VAM3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/cyanoginosin LR, http://linkedlifedata.com/resource/pubmed/chemical/yeast proteinase B inhibitor
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1125-34
pubmed:dateRevised
2009-7-1
pubmed:meshHeading
pubmed-meshheading:9657146-Adenosine Triphosphatases, pubmed-meshheading:9657146-Adenosine Triphosphate, pubmed-meshheading:9657146-Amino Acid Sequence, pubmed-meshheading:9657146-Enzyme Inhibitors, pubmed-meshheading:9657146-Fungal Proteins, pubmed-meshheading:9657146-Glycoproteins, pubmed-meshheading:9657146-Hydrolysis, pubmed-meshheading:9657146-Membrane Fusion, pubmed-meshheading:9657146-Membrane Proteins, pubmed-meshheading:9657146-Microcystins, pubmed-meshheading:9657146-Molecular Sequence Data, pubmed-meshheading:9657146-Mutation, pubmed-meshheading:9657146-Peptides, Cyclic, pubmed-meshheading:9657146-Phosphoprotein Phosphatases, pubmed-meshheading:9657146-Phosphoproteins, pubmed-meshheading:9657146-Protein Binding, pubmed-meshheading:9657146-Qa-SNARE Proteins, pubmed-meshheading:9657146-Saccharomyces cerevisiae, pubmed-meshheading:9657146-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9657146-Thioredoxins, pubmed-meshheading:9657146-Vacuoles, pubmed-meshheading:9657146-Vesicular Transport Proteins
pubmed:year
1998
pubmed:articleTitle
LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion.
pubmed:affiliation
Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't