Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1999-9-7
pubmed:abstractText
Yeast cells of different cell type exhibit distinct budding patterns that reflect the organization of the actin cytoskeleton. Bud1p (Rsr1p), a Ras-like GTPase, and Bud2p, a GTPase-activating protein for Bud1p, are essential for proper budding pattern. We show that Bud2p is localized at the presumptive bud site in G(1) cells in all cell types and that this localization is independent of Bud1p. Bud2p subsequently localizes to the mother-bud neck after bud emergence; this localization depends on the integrity of the septins. These observations indicate that Bud2p becomes positioned in G(1) cells by recognizing cell type-specific landmarks at the presumptive bud site.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-13701687, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-1905981, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-1910037, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-1934633, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-1993729, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-2005793, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-2065354, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-2476649, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-2647769, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-2659436, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-2690082, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-3316985, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-7730409, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-7730410, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-773946, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-7822288, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-7990931, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8262069, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8262070, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8320260, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8371782, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8657162, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8707826, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8723349, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8805277, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8846915, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-8909546, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-9114012, http://linkedlifedata.com/resource/pubmed/commentcorrection/10444589-9843569
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/BUD2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/CDC12 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolase Activators, http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RSR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0890-9369
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1912-7
pubmed:dateRevised
2011-4-1
pubmed:meshHeading
pubmed-meshheading:10444589-Cell Cycle Proteins, pubmed-meshheading:10444589-Cell Division, pubmed-meshheading:10444589-Cell Polarity, pubmed-meshheading:10444589-Cytoskeletal Proteins, pubmed-meshheading:10444589-Fungal Proteins, pubmed-meshheading:10444589-G1 Phase, pubmed-meshheading:10444589-GTP Phosphohydrolase Activators, pubmed-meshheading:10444589-GTP Phosphohydrolases, pubmed-meshheading:10444589-GTPase-Activating Proteins, pubmed-meshheading:10444589-Microscopy, Fluorescence, pubmed-meshheading:10444589-Mutation, pubmed-meshheading:10444589-Proteins, pubmed-meshheading:10444589-Recombinant Fusion Proteins, pubmed-meshheading:10444589-Saccharomyces cerevisiae, pubmed-meshheading:10444589-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10444589-Suppression, Genetic, pubmed-meshheading:10444589-Temperature, pubmed-meshheading:10444589-rab GTP-Binding Proteins, pubmed-meshheading:10444589-ras GTPase-Activating Proteins
pubmed:year
1999
pubmed:articleTitle
Localization of Bud2p, a GTPase-activating protein necessary for programming cell polarity in yeast to the presumptive bud site.
pubmed:affiliation
Department of Molecular Genetics, Ohio State University, Columbus, Ohio 43210-1292, USA. park.294@osu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't