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http://purl.uniprot.org/citations/23708375http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23708375http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23708375http://www.w3.org/2000/01/rdf-schema#comment"The acidic environments in the vacuole and other acidic organelles are important for many cellular processes in eukaryotic cells. In this study, we comprehensively investigated the roles of organelle acidification in vacuolar protein localisation in Saccharomyces cerevisiae. After repressing the acidification of acidic compartments by treatment with concanamycin A, a specific inhibitor of vacuolar H(+)-ATPase (V-ATPase), we examined the localisation of GFP-fused proteins that were predicted to localise in the vacuolar lumen or on the vacuolar membrane. Of the 73 proteins examined, 19 changed their localisation to the cytoplasmic region. Localisation changes were evaluated quantitatively using the image processing programme CalMorph. The delocalised proteins included vacuolar hydrolases, V-ATPase subunits, transporters and enzymes for membrane biogenesis, as well as proteins required for protein transport. These results suggest that many alterations in the localisation of vacuolar proteins occur after loss of the acidification of acidic compartments."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.org/dc/terms/identifier"doi:10.1007/s00709-013-0510-2"xsd:string
http://purl.uniprot.org/citations/23708375http://purl.org/dc/terms/identifier"doi:10.1007/s00709-013-0510-2"xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/author"Matsumoto R."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/author"Matsumoto R."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/author"Ohya Y."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/author"Ohya Y."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/author"Suzuki K."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/author"Suzuki K."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/name"Protoplasma"xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/name"Protoplasma"xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/pages"1283-1293"xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/pages"1283-1293"xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/title"Organelle acidification is important for localisation of vacuolar proteins in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/title"Organelle acidification is important for localisation of vacuolar proteins in Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/volume"250"xsd:string
http://purl.uniprot.org/citations/23708375http://purl.uniprot.org/core/volume"250"xsd:string
http://purl.uniprot.org/citations/23708375http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23708375
http://purl.uniprot.org/citations/23708375http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23708375
http://purl.uniprot.org/citations/23708375http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23708375
http://purl.uniprot.org/citations/23708375http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23708375