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http://purl.uniprot.org/citations/15947196http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15947196http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15947196http://www.w3.org/2000/01/rdf-schema#comment"We demonstrate here that SAP155 encodes a negative modulator of K+ efflux in the yeast Saccharomyces cerevisiae. Overexpression of SAP155 decreases efflux, whereas deletion increases efflux. In contrast, a homolog of SAP155, called SAP185, encodes a positive modulator of K+ efflux: overexpression of SAP185 increases efflux, whereas deletion decreases efflux. Two other homologs, SAP4 and SAP190, are without effect on K+ homeostasis. Both SAP155 and SAP185 require the presence of SIT4 for function, which encodes a PP2A-like phosphatase important for the G1-S transition through the cell cycle. Overexpression of either the outwardly rectifying K+ channel, Tok1p, or the putative plasma membrane K+/H+ antiporter, Kha1p, increases efflux in both wild-type and sit4Delta strains. However, overexpression of the Na+-K+/H+ antiporter, Nha1p, is without effect in a sit4Delta strain, suggesting that Sit4p signals to Nha1p. In summary, the combined activities of Sap155p and Sap185p appear to control the function of Nha1p in K+ homeostasis via Sit4p."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.org/dc/terms/identifier"doi:10.1128/ec.4.6.1041-1049.2005"xsd:string
http://purl.uniprot.org/citations/15947196http://purl.org/dc/terms/identifier"doi:10.1128/ec.4.6.1041-1049.2005"xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/author"Manlandro C.M.A."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/author"Manlandro C.M.A."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/author"Rosenwald A.G."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/author"Rosenwald A.G."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/author"Haydon D.H."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/author"Haydon D.H."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/name"Eukaryot. Cell"xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/name"Eukaryot. Cell"xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/pages"1041-1049"xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/pages"1041-1049"xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/title"Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/title"Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p."xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/15947196http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/15947196http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15947196
http://purl.uniprot.org/citations/15947196http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15947196
http://purl.uniprot.org/citations/15947196http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15947196
http://purl.uniprot.org/citations/15947196http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15947196