title: Std1 and Mth1 proteins interact with the glucose sensors to control glucose-regulated gene expression in Saccharomyces cerevisiae.
abstract: The Std1 protein modulates the expression of glucose-regulated genes, but its exact molecular role in this process is unclear. A two-hybrid screen for Std1-interacting proteins identified the hydrophilic C-terminal domains of the glucose sensors, Snf3 and Rgt2. The homologue of Std1, Mth1, behaves differently from Std1 in this assay by interacting with Snf3 but not Rgt2. Genetic interactions between STD1, MTH1, SNF3, and RGT2 suggest that the glucose signaling is mediated, at least in part, through interactions of the products of these four genes. Mutations in MTH1 can suppress the raffinose growth defect of a snf3 mutant as well as the glucose fermentation defect present in cells lacking both glucose sensors (snf3 rgt2). Genetic suppression by mutations in MTH1 is likely to be due to the increased and unregulated expression of hexose transporter genes. In media lacking glucose or with low levels of glucose, the hexose transporter genes are subject to repression by a mechanism that requires the Std1 and Mth1 proteins. An additional mechanism for glucose sensing must exist since a strain lacking all four genes (snf3 rgt2 std1 mth1) is still able to regulate SUC2 gene expression in response to changes in glucose concentration. Finally, studies with green fluorescent protein fusions indicate that Std1 is localized to the cell periphery and the cell nucleus, supporting the idea that it may transduce signals from the plasma membrane to the nucleus.
authors.affiliation: Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA. mcs2@pop.pitt.edu
authors.forename: M C
authors.initials: MC
authors.lastname: Schmidt
authors.forename: R R
authors.initials: RR
authors.lastname: McCartney
authors.forename: X
authors.initials: X
authors.lastname: Zhang
authors.forename: T S
authors.initials: TS
authors.lastname: Tillman
authors.forename: H
authors.initials: H
authors.lastname: Solimeo
authors.forename: S
authors.initials: S
authors.lastname: Wölfl
authors.forename: C
authors.initials: C
authors.lastname: Almonte
authors.forename: S C
authors.initials: SC
authors.lastname: Watkins
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D015971:Gene Expression Regulation, Enzymologic; D015966:Gene Expression Regulation, Fungal; D005947:Glucose / Q000378:metabolism*; D051246:Glucose Transport Proteins, Facilitative; D006026:Glycoside Hydrolases / Q000235:genetics / Q000378:metabolism; D049452:Green Fluorescent Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008164:Luminescent Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D009004:Monosaccharide Transport Proteins / Q000235:genetics / Q000378:metabolism*; D016296:Mutagenesis; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D043324:beta-Fructofuranosidase
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D005656:Fungal Proteins; D051246:Glucose Transport Proteins, Facilitative; C090594:HXT1 protein, S cerevisiae; D047908:Intracellular Signaling Peptides and Proteins; D008164:Luminescent Proteins; C118806:MTH1 protein, S cerevisiae; D008565:Membrane Proteins; D009004:Monosaccharide Transport Proteins; C112512:RGT2 protein, S cerevisiae; D011993:Recombinant Fusion Proteins; C104463:SNF3 protein, S cerevisiae; C081335:STD1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D049452:Green Fluorescent Proteins; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase; D005947:Glucose