Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1996-4-4
pubmed:abstractText
Here we report the identification of BET3, a new member of a group of interacting genes whose products have been implicated in the targeting and fusion of endoplasmic reticulum (ER) to Golgi transport vesicles with their acceptor compartment. A temperature-sensitive mutant in bet3-1 was isolated in a synthetic lethal screen designed to identify new genes whose products may interact with BET1, a type II integral membrane protein that is required for ER to Golgi transport. At 37 degrees C, bet3-1 fails to transport invertase, alpha-factor, and carboxypeptidase Y from the ER to the Golgi complex. As a consequence, this mutant accumulates dilated ER and small vesicles. The SNARE complex, a docking/fusion complex, fails to form in this mutant. Furthermore, BET3 encodes an essential 22-kDa hydrophilic protein that is conserved in evolution, which is not a component of this complex. These findings support the hypothesis that Bet3p may act before the assembly of the SNARE complex.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-1396561, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-1461285, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-1544568, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-1601878, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-1903184, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-1990290, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2005796, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2007627, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2071670, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2111733, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2192256, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2195039, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2215422, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-237205, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-2657434, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-3049622, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-3312234, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-3323803, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-3390865, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-6996832, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-7026045, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-7039847, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-7199056, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-7923363, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-7990964, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-8028665, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-8157010, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-8196765, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-8280472, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-8455715, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-8455717, http://linkedlifedata.com/resource/pubmed/commentcorrection/8590804-8500167
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1059-1524
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1769-80
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:8590804-Amino Acid Sequence, pubmed-meshheading:8590804-Cloning, Molecular, pubmed-meshheading:8590804-Endoplasmic Reticulum, pubmed-meshheading:8590804-Fungal Proteins, pubmed-meshheading:8590804-Genes, Fungal, pubmed-meshheading:8590804-Golgi Apparatus, pubmed-meshheading:8590804-Kinetics, pubmed-meshheading:8590804-Membrane Proteins, pubmed-meshheading:8590804-Microscopy, Electron, pubmed-meshheading:8590804-Molecular Sequence Data, pubmed-meshheading:8590804-Recombinant Proteins, pubmed-meshheading:8590804-Restriction Mapping, pubmed-meshheading:8590804-SNARE Proteins, pubmed-meshheading:8590804-Saccharomyces cerevisiae, pubmed-meshheading:8590804-Saccharomyces cerevisiae Proteins, pubmed-meshheading:8590804-Sequence Homology, Amino Acid, pubmed-meshheading:8590804-Vesicular Transport Proteins
pubmed:year
1995
pubmed:articleTitle
BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs.
pubmed:affiliation
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't