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      Glucose repression in Saccharomyces cerevisiae

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          Abstract

          Glucose is the primary source of energy for the budding yeast Saccharomyces cerevisiae. Although yeast cells can utilize a wide range of carbon sources, presence of glucose suppresses molecular activities involved in the use of alternate carbon sources as well as it represses respiration and gluconeogenesis. This dominant effect of glucose on yeast carbon metabolism is coordinated by several signaling and metabolic interactions that mainly regulate transcriptional activity but are also effective at post-transcriptional and post-translational levels. This review describes effects of glucose repression on yeast carbon metabolism with a focus on roles of the Snf3/Rgt2 glucose-sensing pathway and Snf1 signal transduction in establishment and relief of glucose repression.

          Abstract

          The role of Snf1 signaling in glucose repression and carbon metabolism in Saccharomyces cerevisae.

          Abstract

          Graphical Abstract Figure.

          The role of Snf1 signaling in glucose repression and carbon metabolism in Saccharomyces cerevisae.

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          Global analysis of protein phosphorylation in yeast.

          Jason Ptacek, Geeta Devgan, Gregory Michaud … (2005)
          Protein phosphorylation is estimated to affect 30% of the proteome and is a major regulatory mechanism that controls many basic cellular processes. Until recently, our biochemical understanding of protein phosphorylation on a global scale has been extremely limited; only one half of the yeast kinases have known in vivo substrates and the phosphorylating kinase is known for less than 160 phosphoproteins. Here we describe, with the use of proteome chip technology, the in vitro substrates recognized by most yeast protein kinases: we identified over 4,000 phosphorylation events involving 1,325 different proteins. These substrates represent a broad spectrum of different biochemical functions and cellular roles. Distinct sets of substrates were recognized by each protein kinase, including closely related kinases of the protein kinase A family and four cyclin-dependent kinases that vary only in their cyclin subunits. Although many substrates reside in the same cellular compartment or belong to the same functional category as their phosphorylating kinase, many others do not, indicating possible new roles for several kinases. Furthermore, integration of the phosphorylation results with protein-protein interaction and transcription factor binding data revealed novel regulatory modules. Our phosphorylation results have been assembled into a first-generation phosphorylation map for yeast. Because many yeast proteins and pathways are conserved, these results will provide insights into the mechanisms and roles of protein phosphorylation in many eukaryotes.
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            Gene expression is circular: factors for mRNA degradation also foster mRNA synthesis.

            Gonzalo Millán-Zambrano, Sebastien Z Causse, Oren Barkai … (2013)
            Maintaining proper mRNA levels is a key aspect in the regulation of gene expression. The balance between mRNA synthesis and decay determines these levels. We demonstrate that most yeast mRNAs are degraded by the cytoplasmic 5'-to-3' pathway (the "decaysome"), as proposed previously. Unexpectedly, the level of these mRNAs is highly robust to perturbations in this major pathway because defects in various decaysome components lead to transcription downregulation. Moreover, these components shuttle between the cytoplasm and the nucleus, in a manner dependent on proper mRNA degradation. In the nucleus, they associate with chromatin-preferentially ∼30 bp upstream of transcription start-sites-and directly stimulate transcription initiation and elongation. The nuclear role of the decaysome in transcription is linked to its cytoplasmic role in mRNA decay; linkage, in turn, seems to depend on proper shuttling of its components. The gene expression process is therefore circular, whereby the hitherto first and last stages are interconnected. Copyright © 2013 Elsevier Inc. All rights reserved.
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              Function and regulation of yeast hexose transporters.

              Jeffrey M. Johnston, Mehmet S. Ozcan (1999)
              Glucose, the most abundant monosaccharide in nature, is the principal carbon and energy source for nearly all cells. The first, and rate-limiting, step of glucose metabolism is its transport across the plasma membrane. In cells of many organisms glucose ensures its own efficient metabolism by serving as an environmental stimulus that regulates the quantity, types, and activity of glucose transporters, both at the transcriptional and posttranslational levels. This is most apparent in the baker's yeast Saccharomyces cerevisiae, which has 20 genes encoding known or likely glucose transporters, each of which is known or likely to have a different affinity for glucose. The expression and function of most of these HXT genes is regulated by different levels of glucose. This review focuses on the mechanisms S. cerevisiae and a few other fungal species utilize for sensing the level of glucose and transmitting this information to the nucleus to alter HXT gene expression. One mechanism represses transcription of some HXT genes when glucose levels are high and works through the Mig1 transcriptional repressor, whose function is regulated by the Snf1-Snf4 protein kinase and Reg1-Glc7 protein phosphatase. Another pathway induces HXT expression in response to glucose and employs the Rgt1 transcriptional repressor, a ubiquitin ligase protein complex (SCF(Grr1)) that regulates Rgt1 function, and two glucose sensors in the membrane (Snf3 and Rgt2) that bind glucose and generate the intracellular signal to which Rgt1 responds. These two regulatory pathways collaborate with other, less well-understood, pathways to ensure that yeast cells express the glucose transporters best suited for the amount of glucose available.
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                Author and article information

                Journal
                Journal ID (nlm-ta): FEMS Yeast Res
                Journal ID (iso-abbrev): FEMS Yeast Res
                Journal ID (hwp): femsyr
                Journal ID (publisher-id): femsyr
                Title: FEMS Yeast Research
                Publisher: Oxford University Press
                ISSN (Print): 1567-1356
                ISSN (Electronic): 1567-1364
                Publication date (Electronic): 23 July 2015
                Publication date (Print): September 2015
                Publication date PMC-release: 23 July 2015
                Volume: 15
                Issue: 6
                Electronic Location Identifier: fov068
                Affiliations
                [1 ]Department of Biology and Biological Engineering, Kemivägen 10, Chalmers University of Technology, SE41296 Gothenburg, Sweden
                [2 ]Novo Nordisk Foundation Center for Biosustainability, Chalmers University of Technology, SE41296 Gothenburg, Sweden
                [3 ]Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, DK2970 Hørsholm, Denmark
                Author notes
                [* ] Corresponding author: Department of Biology and Biological Engineering, Kemivägen 10, Chalmers University of Technology, SE41296 Gothenburg, Sweden. Tel: +46 (0) 31 772 3804; E-mail: nielsenj@ 123456chalmers.se
                Article
                DOI: 10.1093/femsyr/fov068
                PMC ID: 4629793
                PubMed ID: 26205245
                SO-VID: 0c3b7e91-7f45-49e6-8032-9ae0929f8a3e
                Copyright © © FEMS 2015.
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date accepted : 20 July 2015
                Date revision received : 12 March 2015
                Page count
                Pages: 8
                Categories
                Subject: Minireview
                Custom metadata
                cover-date September 2015

                ScienceOpen disciplines: Molecular biology
                Keywords: carbon metabolism,snf1 signaling,carbon catabolite repression
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: carbon metabolism, snf1 signaling, carbon catabolite repression

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