Endocytosis and Vacuolar Degradation of the Yeast Cell Surface Glucose Sensors Rgt2 and Snf3

Roy, Adhiraj; Kim, Jeong-Ho

doi:10.1074/jbc.m113.539411

Cited by 13 publications

(18 citation statements)

References 49 publications

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“…However, inhibition of glycolysis did not further affect Rag4 or Rgt2 localization when cells were grown in the presence of glycerol or galactose. Our finding showing that Rag4 and Rgt2 localizations are controlled by the carbon source is in agreement with a recent report showing that the stability of Snf3 and Rgt2 glucose sensors in S. cerevisiae is regulated by the concentration of extracellular glucose (33). Hence, Snf3 and Rgt2 are stabilized at the plasma membrane when the extracellular glucose concentration is in the range of their respective affinities.…”

Section: Discussionsupporting

confidence: 81%

“…Indeed, our observations that both Rag4 and Rgt2 are not stable in glucose-grown cells when the level of glycolysis is reduced suggest that the intracellular glycolytic signal may overcome the effect of extracellular glucose binding to the glucose sensors. Finally, Roy and Kim further suggest that Rgt2 stability is controlled via Rsp5-dependent ubiquitination of two lysine residues located in the Rgt2 C-terminal cytosolic extension, a region characteristic of the glucose sensors of yeasts (8,19,(33)(34)(35). Sequence alignment and computational analysis of these C-terminal extensions revealed that the two lysines important for Rgt2 stability are not conserved in Rag4 (our unpublished data).…”

Section: Discussionmentioning

confidence: 99%

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Glycolysis Controls Plasma Membrane Glucose Sensors To Promote Glucose Signaling in Yeasts

Cairey-Remonnay

Deffaud

Wésolowski-Louvel

et al. 2015

Molecular and Cellular Biology

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Sensing of extracellular glucose is necessary for cells to adapt to glucose variation in their environment. In the respiratory yeast Kluyveromyces lactis, extracellular glucose controls the expression of major glucose permease gene RAG1 through a cascade similar to the Saccharomyces cerevisiae Snf3/Rgt2/Rgt1 glucose signaling pathway. This regulation depends also on intracellular glucose metabolism since we previously showed that glucose induction of the RAG1 gene is abolished in glycolytic mutants. Here we show that glycolysis regulates RAG1 expression through the K. lactis Rgt1 (KlRgt1) glucose signaling pathway by targeting the localization and probably the stability of Rag4, the single Snf3/Rgt2-type glucose sensor of K. lactis. Additionally, the control exerted by glycolysis on glucose signaling seems to be conserved in S. cerevisiae. This retrocontrol might prevent yeasts from unnecessary glucose transport and intracellular glucose accumulation. Sensing and adaption to environmental variations and stresses is fundamental for any cell to live and to grow properly. Among the environmental signals that cells have to consider, nutrients, and especially glucose, are of particular importance. Indeed, glucose is the principal carbon and energy source for most living organisms. Glucose signaling is a key pathway allowing cells to adapt their sugar transport system and metabolism to the quality and quantity of carbon source present in their environment.Glucose transport and the glucose signaling network have been widely studied in the fermentative yeast model Saccharomyces cerevisiae (1). The yeast Kluyveromyces lactis is an excellent alternate and complementary model organism to investigate glucose signaling (2). Indeed, the pathway is simpler, with only two glucose permeases and little if any gene redundancy. Moreover, unlike S. cerevisiae, the K. lactis living style is preferably respiratory, making it closer to superior eukaryotes. In K. lactis, the fermentative growth on medium containing 5% glucose plus antimycin A (respiration inhibitor) defines the Rag-positive (Rag ϩ ) phenotype and is informative about the functionality of glucose signaling, glucose transport, and glucose metabolism.In K. lactis, two glucose permeases are known: Rag1, with a low affinity for glucose, and Hgt1, having a high affinity for glucose (3,4). Only RAG1 expression is regulated by the extracellular glucose concentration (5). In the absence of extracellular glucose, the transcriptional repressor K. lactis Rgt1 (KlRgt1), bound to the corepressor Sms1, represses RAG1 expression (6, 7) (see Fig. 1A for a model). Extracellular glucose is sensed by the plasma membrane glucose sensor Rag4, a glucose permease homolog unable to transport glucose (8) and exhibiting a characteristic long cytoplasmic C-terminal tail thought to have a role in glucose signaling. Glucose binding to Rag4 probably leads to a conformational change allowing interaction with the casein kinase I (CKI) Rag8 (6, 9). When activated by glucose, Rag8 is supposed to phosphor...

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Section: Discussionsupporting

confidence: 81%

Section: Discussionmentioning

confidence: 99%

Glycolysis Controls Plasma Membrane Glucose Sensors To Promote Glucose Signaling in Yeasts

Cairey-Remonnay

Deffaud

Wésolowski-Louvel

et al. 2015

Molecular and Cellular Biology

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“…The Rgt2 high-affinity glucose sensor is stabilized by glucose and is degraded in the absence of glucose through its ubiquitination and consequent targeting to the vacuole (Roy and Kim, 2014), and Yck-dependent phosphorylation of the uracil permease Fur4 within a PEST sequence stimulates its ubiquitination and degradation (Marchal et al , 2000). The C-terminal region of Rgt2 near box1, where Yck-dependent phosphorylation occurs, resembles a PEST sequence that we surmised could function to regulate the stability of Rgt2.…”

Section: Resultsmentioning

confidence: 99%

“…Knowing that the Ycks are required for stability of several membrane proteins, including transporters and permeases, and that Rgt2 and Snf3 are turned over in response to low and high glucose levels, respectively (Roy and Kim, 2014), we were surprised to find that Rgt2 is stable in a yck1∆yck2 ts mutant and that mutation of the Yck-dependent phosphorylation sites of Rgt2 does not affect its stability (even though the phosphorylation sites on Rgt2 are in a region that resembles a PEST degradation sequence).…”

Section: Discussionmentioning

confidence: 99%

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A novel role for yeast casein kinases in glucose sensing and signaling

Snowdon

Johnston

2016

MBoC

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Lactic acid production from cellobiose and xylose by engineered Saccharomyces cerevisiae

Turner

Zhang

et al. 2015

Biotech & Bioengineering

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Efficient and rapid production of value-added chemicals from lignocellulosic biomass is an important step toward a sustainable society. Lactic acid, used for synthesizing the bioplastic polylactide, has been produced by microbial fermentation using primarily glucose. Lignocellulosic hydrolysates contain high concentrations of cellobiose and xylose. Here, we constructed a recombinant Saccharomyces cerevisiae strain capable of fermenting cellobiose and xylose into lactic acid. Specifically, genes (cdt-1, gh1-1, XYL1, XYL2, XYL3, and ldhA) coding for cellobiose transporter, β-glucosidase, xylose reductase, xylitol dehydrogenase, xylulokinase, and lactate dehydrogenase were integrated into the S. cerevisiae chromosomes. The resulting strain produced lactic acid from cellobiose or xylose with high yields. When fermenting a cellulosic sugar mixture containing 10 g/L glucose, 40 g/L xylose, and 80 g/L cellobiose, the engineered strain produced 83 g/L of lactic acid with a yield of 0.66 g lactic acid/g sugar (66% theoretical maximum). This study demonstrates initial steps toward the feasibility of sustainable production of lactic acid from lignocellulosic sugars by engineered yeast.

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Endocytosis and Vacuolar Degradation of the Yeast Cell Surface Glucose Sensors Rgt2 and Snf3

Cited by 13 publications

References 49 publications

Glycolysis Controls Plasma Membrane Glucose Sensors To Promote Glucose Signaling in Yeasts

Glycolysis Controls Plasma Membrane Glucose Sensors To Promote Glucose Signaling in Yeasts

A novel role for yeast casein kinases in glucose sensing and signaling

Lactic acid production from cellobiose and xylose by engineered Saccharomyces cerevisiae

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