Yeast PKA represses Msn2p/Msn4p-dependent gene expression to regulate growth, stress response and glycogen accumulation

Smith, A.M.

doi:10.1093/emboj/17.13.3556

Cited by 335 publications

(386 citation statements)

References 43 publications

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“…A recent report suggests that Yak1 phosphorylates and thereby activates Msn2 through a still unknown mechanism, which apparently does not implicate the control of Msn2 subcellular localization (Lee et al 2008a). Since the YAK1 gene itself is induced by Msn2/4, this would generate a positive feedback loop (Smith et al 1998). In the same study, Yak1 was also found to stimulate the activity of Hsf1, another transcriptional activator of stress response genes that was recently shown to be under negative control of PKA (Hahn et al 2004;Ferguson et al 2005;Lee et al 2008a).…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

“…Two of those are the transcription factors Msn2 and Msn4, which mediate the transcription of the so-called stress response element (STRE)-controlled genes (Estruch and Carlson 1993;Martinez-Pastor et al 1996;Schmitt and McEntee 1996). STRE genes are involved in a wide variety of processes, including protection against diverse types of stress such as heat, oxidative and osmotic stress, carbohydrate metabolism and growth regulation (Mai and Breeden 1997;Moskvina et al 1998;Smith et al 1998;Gasch et al 2000). Msn2 and Msn4 are inhibited by PKA and, notably, deletion of both MSN2 and MSN4 rescues the lethality of a tpk null strain (Boy-Marcotte et al 1998;Smith et al 1998).…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

“…STRE genes are involved in a wide variety of processes, including protection against diverse types of stress such as heat, oxidative and osmotic stress, carbohydrate metabolism and growth regulation (Mai and Breeden 1997;Moskvina et al 1998;Smith et al 1998;Gasch et al 2000). Msn2 and Msn4 are inhibited by PKA and, notably, deletion of both MSN2 and MSN4 rescues the lethality of a tpk null strain (Boy-Marcotte et al 1998;Smith et al 1998). During growth on glucose, Msn2 and Msn4 are phosphorylated and reside in the cytosol.…”

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%

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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“…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 Amentioning

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 effect of Ras underlies most, if not all of Ras-induced phenotypes in yeast (Sass et al, 1986;Smith et al, 1998;Stanhill et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Ha-rasval12 induces HSP70b transcription via the HSE/HSF1 system, but HSP70b expression is suppressed in Ha-rasval12-transformed cells

et al. 2005

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Heat shock proteins (Hsps) are overexpressed in many tumors, but are downregulated in some tumors. To check for a direct effect of Ha-Ras val12 on HSP70 transcription, we transiently expressed the oncoprotein in Rat1 fibroblasts and monitored its effect on HSP70b promoterdriven reporter gene. We show that expression of Ha-Ras val12 induced this promoter. Promoter analysis via systematic deletions and point mutations revealed that Ha-Ras val12 induces HSP70b transcription via heat shock elements (HSEs). Also, Ha-Ras val12 induction of HSEmediated transcription was dramatically reduced in HSF1À/À cells. Yet, residual effect of Ha-Ras val12 that was still measured in HSF1À/À cells suggests that some of the Ha-Ras val12 effect is Hsf1-independent. When HSF1À/À cells, stably expressing Ha-Ras val12 , were grown on soft agar only small colonies were formed suggesting a role for heat shock factor 1 (Hsf1) in Ha-Ras val12 -mediated transformation. Although Ha-ras Val12 seems to be an inducer of HSP70's expression, we found that in Ha-ras Val12-transformed fibroblasts expression of this gene is suppressed. This suppression is correlated with higher sensitivity of Ha-ras val12 -transformed cells to heat shock. We suggest that Ha-ras Val12 is involved in Hsf1 activation, thereby inducing the cellular protective response. Cells that repress this response are perhaps those that acquire the capability to further proliferate and become transformed clones.

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Yeast PKA represses Msn2p/Msn4p-dependent gene expression to regulate growth, stress response and glycogen accumulation

Cited by 335 publications

References 43 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

Ha-rasval12 induces HSP70b transcription via the HSE/HSF1 system, but HSP70b expression is suppressed in Ha-rasval12-transformed cells

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