title: Hexose phosphorylation and the putative calcium channel component Mid1p are required for the hexose-induced transient elevation of cytosolic calcium response in Saccharomyces cerevisiae.
abstract: Saccharomyces cerevisiae responds to environ-mental stimuli such as an exposure to pheromone or to hexoses after carbon source limitation with a transient elevation of cytosolic calcium (TECC) response. In this study, we examined whether hexose transport and phosphorylation are necessary for the TECC response. We found that a mutant strain lacking most of the known hexose transporters was unable to carry out the TECC response when exposed to glucose. A mutant strain that lacked the ability to phosphorylate glucose was unable to respond to glucose addition, but displayed a normal TECC response after the addition of galactose. These results indicate that hexose uptake and phosphorylation are required to trigger the hexose-induced TECC response. We also found that the TECC response was significantly smaller than normal when the level of environmental calcium was reduced, and was abolished in a mid1 mutant that lacked a subunit of the high-affinity calcium channel of the yeast plasma membrane. These results indicate that most or all of the TECC response is mediated by an influx of calcium from the extracellular space. Our results indicate that this transient increase in plasma membrane calcium permeability may be linked to the accumulation of Glc-1-P (or a related glucose metabolite) in yeast.
authors.affiliation: Department of Clinical Chemistry, Faculty of Medicine, Pécs University, 13 Ifjuság u., Pécs 7624, Hungary.
authors.forename: Margit
authors.initials: M
authors.lastname: Tökés-Füzesi
authors.forename: David M
authors.initials: DM
authors.lastname: Bedwell
authors.forename: Imre
authors.initials: I
authors.lastname: Repa
authors.forename: Katalin
authors.initials: K
authors.lastname: Sipos
authors.forename: Balázs
authors.initials: B
authors.lastname: Sümegi
authors.forename: András
authors.initials: A
authors.lastname: Rab
authors.forename: Attila
authors.initials: A
authors.lastname: Miseta
mesh_terms: D000331:Aequorin / Q000235:genetics / Q000378:metabolism; D002118:Calcium / Q000378:metabolism*; D015220:Calcium Channels / Q000378:metabolism*; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D017930:Genes, Reporter; D019298:Glucose-6-Phosphate / Q000378:metabolism; D005958:Glucosephosphates / Q000378:metabolism; D006601:Hexoses / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D009004:Monosaccharide Transport Proteins / Q000235:genetics / Q000378:metabolism; D010733:Phosphoglucomutase / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D015220:Calcium Channels; D005656:Fungal Proteins; D005958:Glucosephosphates; D006601:Hexoses; C090463:MID1 protein, S cerevisiae; D008562:Membrane Glycoproteins; D009004:Monosaccharide Transport Proteins; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D000331:Aequorin; D019298:Glucose-6-Phosphate; C031590:glucose-1-phosphate; D010733:Phosphoglucomutase; D002118:Calcium