A <i>Saccharomyces cerevisiae</i> G‐protein coupled receptor, Gpr1, is specifically required for glucose activation of the cAMP pathway during the transition to growth on glucose

Kraakman, L.; Lemaire, Katleen; Packham, MA; Teunissen, Aloys; Donaton, M.; Dijck, Patrick Van; Winderickx, Joris; Winde, Johannes H. de; Thevelein, Johan M.

doi:10.1046/j.1365-2958.1999.01413.x

Cited by 325 publications

(364 citation statements)

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“…Extracellular glucose detection occurs through a G protein-coupled receptor (GPCR) system, composed of Gpr1 and Gpa2 (Kraakman et al 1999a). Gpr1 belongs to the G protein-coupled seven-transmembrane receptor (GPCR) superfamily (Yun et al 1997;Xue et al 1998) and Gpa2 is a member of the heterotrimeric G protein a subunit (G a ) protein family (Nakafuku et al 1988).…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

“…Gpr1 belongs to the G protein-coupled seven-transmembrane receptor (GPCR) superfamily (Yun et al 1997;Xue et al 1998) and Gpa2 is a member of the heterotrimeric G protein a subunit (G a ) protein family (Nakafuku et al 1988). Addition of glucose to derepressed cells activates Gpr1, which in turn stimulates the exchange of GDP for GTP on Gpa2 (Kraakman et al 1999a). The Gpr1-Gpa2 couple displays a rather low affinity for glucose, with a halfmaximum response (EC 50 ) of 20-75 mM, depending on the genetic background tested and the experimental setup Lemaire et al 2004).…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

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Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

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Cells of all living organisms contain complex signal transduction networks to ensure that a wide range of physiological properties are properly adapted to the environmental conditions. The fundamental concepts and individual building blocks of these signalling networks are generally well-conserved from yeast to man; yet, the central role that growth factors and hormones play in the regulation of signalling cascades in higher eukaryotes is executed by nutrients in yeast. Several nutrient-controlled pathways, which regulate cell growth and proliferation, metabolism and stress resistance, have been defined in yeast. These pathways are integrated into a signalling network, which ensures that yeast cells enter a quiescent, resting phase (G 0 ) to survive periods of nutrient scarceness and that they rapidly resume growth and cell proliferation when nutrient conditions become favourable again. A series of well-conserved nutrient-sensory protein kinases perform key roles in this signalling network: i.e. Snf1, PKA, Tor1 and Tor2, Sch9 and Pho85-Pho80. In this review, we provide a comprehensive overview on the current understanding of the signalling processes mediated via these kinases with a particular focus on how these individual pathways converge to signalling networks that ultimately ensure the dynamic translation of extracellular nutrient signals into appropriate physiological responses.

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Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

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“…Plasmid YEplac181-GPA2 Val132 or YEplac181-GPA2 Ala273 (Kraakman et al, 1999) were used to transform W303 cells to obtain strains W-GPA2 V132 and W-GPA2 A273 . Strain W-GUS (W303 background) was obtained by transformation with the integrative plasmid pKV3-d2 containing the HSP12 promoter region fused to the GUS reporter gene (Varela, Praekelt, Meacock, Planta, & Mager, 1995).…”

Section: Strains Growth Media and Plasmidsmentioning

confidence: 99%

“…The fast activation of the Ras-cAMP pathway triggered by glucose addition results in mobilization of storage carbohydrates (Francois, Villanueva, & Hers, 1998;Kraakman et al, 1999;Smith, Ward, & Garrett, 1998;Van der Plaat, 1974), such as glycogen, and increased heat-shock sensitivity, partly mediated by the rapid shutdown of genes containing STRE elements in their promoters (Moskivna, Schuller, Mauer, Mager, & Ruis, 1998;Ruis & Schuller, 1995). Stp1 expressing cells growing on synthetic media supplemented with a non-fermentable carbon source, accumulate higher levels of intracellular glycogen than their wild-type counterparts.…”

Section: The Phenotype Of Cells Expressing Stp1 Is Consistent With a mentioning

confidence: 99%

In Saccharomyces cerevisiae an unbalanced level of tyrosine phosphorylation down-regulates the Ras/PKA pathway

Magherini

Busti

Gamberi

et al. 2006

The International Journal of Biochemistry & Cell Biology

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The role of tyrosyl phosphorylation/dephosphorylation in the budding yeast Saccharomyces cerevisiae, whose genome does not encode typical tyrosyne kinases, has long remained elusive. Nevertheless, several protein kinases phosphorylating poly(TyrGlu) substrates have been identified. In this work, we use the expression of the low molecular weight tyrosine phosphatase Stp1 from the distantly related yeast Schizosaccharomyces pombe, as a tool to investigate whether an unbalanced level of protein tyrosine phosphorylation affects S. cerevisiae growth and metabolism. We correlate the previously reported down-regulation of the phosphotyrosine level brought about by overexpression of Stp1 with a large number of phenotypes indicative of down-regulation of the Ras pathway. These phenotypes include reduction in both glucose-and acidification-induced GTP loading of the Ras2 protein and cAMP signaling, impaired growth on a non-fermentable carbon source, alteration of cell cycle parameters, delayed recovery from nitrogen starvation, increased heat-shock resistance, attenuated pseudohyphal and invasive growth. Genetic data suggest that Stp1 acts either at, or above, the level of Ras2, possibly on the Ira proteins. Consistently, Stp1 was found to bind to immunoprecipitated Ira2. Since a catalytically inactive mutant form of Stp1 (Stp1 C11S ) effectively binds to Ira2 without producing any effect on yeast physiology, we conclude that down-regulation of the Ras pathway by Stp1 requires its phosphatase activity. In conclusion, our data suggest a possible cross-talk between tyrosine phosphorylation and the Ras pathway in yeast.

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“…This transient increase is strongly reduced in a strain with enhanced feedback inhibition of cAMP synthesis by elevated cAPK activity (Mbonyi et al, 1990;Colombo et al, 1998; Figure 1B), such as a bcy1 disruptant, which is also defective in the slow adaptation of the actin cytoskeleton in the absence of glucose (see above). In addition, the transient increase is also partially dependent on Gpr1p, a putative G protein-coupled receptor, and Gpa2p, a G protein subunit (Thevelein, 1984;Kü bler et al, 1997;Kraakman et al, 1999). To ask whether this transient increase of cAMP is required for the recovery of actin polarization upon glucose addition, we observed the recovery in bcy1, gpr1, and gpa2 disruptants.…”

Section: Recovery Of Actin Polarization Upon Glucose Readdition Does mentioning

confidence: 99%

Simultaneous yet Independent Regulation of Actin Cytoskeletal Organization and Translation Initiation by Glucose inSaccharomyces cerevisiae

Uesono

Ashe

Toh‐e

2004

MBoC

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Acute glucose deprivation rapidly but transiently depolarizes the actin cytoskeleton and inhibits translation initiation in Saccharomyces cerevisiae. Neither rapid actin depolarization nor translation inhibition upon glucose removal occurs in a reg1 disruptant, which is defective in glucose repression, or in the tpk1 w mutant, which has weak cAPK activity. In the absence of additional glucose, recovery of either actin polarization or translation initiation relies upon respiration, the Snf1p protein kinase, and the transcription factors Msn2p and Msn4p. The readdition of glucose to glucose-starved cells causes a rapid recovery of actin polarization as well as translation initiation without respiration. These results indicate that the simultaneous regulation of actin polarization and translation initiation is divided into three reactions: 1) rapid shutdown depending on Reg1p and cAPK after glucose removal, 2) slow adaptation depending on Snf1p and Msn2p/4p in the absence of glucose, and 3) rapid recovery upon readdition of glucose. On glucose removal, translation initiation is rapidly inhibited in a rom2 disruptant, which is defective in rapid actin depolarization, whereas rapid actin depolarization occurs in a pop2/caf1 disruptant, which is defective in rapid inhibition of translation initiation. Thus, translation initiation and actin polarization seem to be simultaneously but independently regulated by glucose deprivation. INTRODUCTIONThe actin cytoskeleton provides the structural basis for cell polarity in the yeast Saccharomyces cerevisiae and is organized primarily into two morphologically distinct structures: cortical patches and cables (Botstein et al., 1997). Cortical patches are discrete cytoskeletal bodies at the plasma membrane, whereas actin cables are long bundles of actin filaments that are oriented along the mother-bud axis. Both structures are polarized during the budding phase of the cell cycle. During early G1 phase, cortical patches and cables are randomly distributed. As a bud emerges, cortical patches cluster at the growing tip and cables extend from the mother cell into the bud. Near the end of bud growth, the patches and cables redistribute randomly, disrupting the asymmetric distribution of the actin cytoskeleton. At the end of mitosis, patches accumulate in and cables reorient toward the mother-bud neck in connection with cytokinesis and septum formation (Botstein et al., 1997).The actin cytoskeleton is also regulated in response to environmental stimuli. Mating pheromone causes polarization of the actin cytoskeleton toward the tip of the mating projection via the Cdc42p GTPase (Read et al., 1992;Leberer et al., 1997). In contrast, stresses such as osmotic shock, heat shock, and glucose starvation depolarize the actin cytoskeleton in budded cells as shown in Figure 1A (Novick et al., 1989;Chowdhury et al., 1992;Delley and Hall, 1999). In particular, the depolarization by heat or osmotic stress is known to be a rapid and transient reaction. A recent report has indicated that the rapid depol...

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A Saccharomyces cerevisiae G‐protein coupled receptor, Gpr1, is specifically required for glucose activation of the cAMP pathway during the transition to growth on glucose

Cited by 325 publications

References 50 publications

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

In Saccharomyces cerevisiae an unbalanced level of tyrosine phosphorylation down-regulates the Ras/PKA pathway

Simultaneous yet Independent Regulation of Actin Cytoskeletal Organization and Translation Initiation by Glucose inSaccharomyces cerevisiae

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