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http://purl.uniprot.org/citations/15252028http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15252028http://www.w3.org/2000/01/rdf-schema#comment"Loss of the major isoform of phosphoglucomutase (PGM) causes an accumulation of glucose 1-phosphate when yeast cells are grown with galactose as the carbon and energy source. Remarkably, the pgm2Delta strain also exhibits a severe imbalance in intracellular Ca(2+) homeostasis when grown under these conditions. In the present study, we examined how the pgm2Delta mutation alters yeast Ca(2+) homeostasis in greater detail. We found that a shift from glucose to galactose as the carbon source resulted in a 2-fold increase in the rate of cellular Ca(2+) uptake in wild-type cells, whereas Ca(2+) uptake increased 8-fold in the pgm2Delta mutant. Disruption of the PMC1 gene, which encodes the vacuolar Ca(2+)-ATPase Pmc1p, suppressed the Ca(2+)-related phenotypes observed in the pgm2Delta strain. This suggests that excessive vacuolar Ca(2+) uptake is tightly coupled to these defects in Ca(2+) homeostasis. An in vitro assay designed to measure Ca(2+) sequestration into intracellular compartments confirmed that the pgm2Delta mutant contained a higher level of Pmc1p-dependent Ca(2+) transport activity than the wild-type strain. We found that this increased rate of vacuolar Ca(2+) uptake also coincided with a large induction of the unfolded protein response in the pgm2Delta mutant, suggesting that Ca(2+) uptake into the endoplasmic reticulum compartment was reduced. These results indicate that the excessive Ca(2+) uptake and accumulation previously shown to be associated with the pgm2Delta mutation are due to a severe imbalance in the distribution of cellular Ca(2+) into different intracellular compartments."xsd:string
http://purl.uniprot.org/citations/15252028http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m400833200"xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/author"Fu L."xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/author"Aiello D.P."xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/author"Bedwell D.M."xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/author"Sipos K."xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/author"Miseta A."xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/pages"38495-38502"xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/title"The Ca2+ homeostasis defects in a pgm2Delta strain of Saccharomyces cerevisiae are caused by excessive vacuolar Ca2+ uptake mediated by the Ca2+-ATPase Pmc1p."xsd:string
http://purl.uniprot.org/citations/15252028http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15252028http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15252028
http://purl.uniprot.org/citations/15252028http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15252028
http://purl.uniprot.org/uniprot/P37012#attribution-5EF7E011C1A86C4BEA47CDBF7746F02Ahttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15252028
http://purl.uniprot.org/uniprot/#_P37012-mappedCitation-15252028http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15252028
http://purl.uniprot.org/uniprot/#_P38929-mappedCitation-15252028http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15252028
http://purl.uniprot.org/uniprot/P38929http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15252028
http://purl.uniprot.org/uniprot/P37012http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15252028