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Articles de revues sur le sujet « Saccharomyces cerevisiae Signal Transduction »

Auteur : Grafiati

Publié le 4 juin 2021

Mis à jour le 1 février 2022

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1

Portela, P., and Silvia Rossi. "cAMP-PKA signal transduction specificity in Saccharomyces cerevisiae." Current Genetics 66, no. 6 (2020): 1093–99. http://dx.doi.org/10.1007/s00294-020-01107-6.

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Oehlen, Bert, and Frederick R. Cross. "Signal transduction in the budding yeast Saccharomyces cerevisiae." Current Opinion in Cell Biology 6, no. 6 (1994): 836–41. http://dx.doi.org/10.1016/0955-0674(94)90053-1.

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Pan, Xuewen, Toshiaki Harashima, and Joseph Heitman. "Signal transduction cascades regulating pseudohyphal differentiation of Saccharomyces cerevisiae." Current Opinion in Microbiology 3, no. 6 (2000): 567–72. http://dx.doi.org/10.1016/s1369-5274(00)00142-9.

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Magasanik, B. "The transduction of the nitrogen regulation signal in Saccharomyces cerevisiae." Proceedings of the National Academy of Sciences 102, no. 46 (2005): 16537–38. http://dx.doi.org/10.1073/pnas.0507116102.

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Kaniak, Aneta, Zhixiong Xue, Daniel Macool, Jeong-Ho Kim, and Mark Johnston. "Regulatory Network Connecting Two Glucose Signal Transduction Pathways in Saccharomyces cerevisiae." Eukaryotic Cell 3, no. 1 (2004): 221–31. http://dx.doi.org/10.1128/ec.3.1.221-231.2004.

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ABSTRACT The yeast Saccharomyces cerevisiae senses glucose, its preferred carbon source, through multiple signal transduction pathways. In one pathway, glucose represses the expression of many genes through the Mig1 transcriptional repressor, which is regulated by the Snf1 protein kinase. In another pathway, glucose induces the expression of HXT genes encoding glucose transporters through two glucose sensors on the cell surface that generate an intracellular signal that affects function of the Rgt1 transcription factor. We profiled the yeast transcriptome to determine the range of genes target

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Choi, You-Jeong, Sun-Hong Kim, Ki-Sook Park, and Kang-Yell Choi. "Differential transmission of G1 cell cycle arrest and mating signals by Saccharomyces cerevisiae Ste5 mutants in the pheromone pathway." Biochemistry and Cell Biology 77, no. 5 (1999): 459–68. http://dx.doi.org/10.1139/o99-054.

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Saccharomyces cerevisiae Ste5 is a scaffold protein that recruits many pheromone signaling molecules to sequester the pheromone pathway from other homologous mitogen-activated protein kinase pathways. G1 cell cycle arrest and mating are two different physiological consequences of pheromone signal transduction and Ste5 is required for both processes. However, the roles of Ste5 in G1 arrest and mating are not fully understood. To understand the roles of Ste5 better, we isolated 150 G1 cell cycle arrest defective STE5 mutants by chemical mutagenesis of the gene. Here, we found that two G1 cell cy

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Moskow, John J., Amy S. Gladfelter, Rachel E. Lamson, Peter M. Pryciak, and Daniel J. Lew. "Role of Cdc42p in Pheromone-Stimulated Signal Transduction in Saccharomyces cerevisiae." Molecular and Cellular Biology 20, no. 20 (2000): 7559–71. http://dx.doi.org/10.1128/mcb.20.20.7559-7571.2000.

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ABSTRACT CDC42 encodes a highly conserved GTPase of the Rho family that is best known for its role in regulating cell polarity and actin organization. In addition, various studies of both yeast and mammalian cells have suggested that Cdc42p, through its interaction with p21-activated kinases (PAKs), plays a role in signaling pathways that regulate target gene transcription. However, recent studies of the yeast pheromone response pathway suggested that prior results with temperature-sensitive cdc42 mutants were misleading and that Cdc42p and the Cdc42p-PAK interaction are not involved in signal

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Santangelo, George M. "Glucose Signaling in Saccharomyces cerevisiae." Microbiology and Molecular Biology Reviews 70, no. 1 (2006): 253–82. http://dx.doi.org/10.1128/mmbr.70.1.253-282.2006.

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SUMMARY Eukaryotic cells possess an exquisitely interwoven and fine-tuned series of signal transduction mechanisms with which to sense and respond to the ubiquitous fermentable carbon source glucose. The budding yeast Saccharomyces cerevisiae has proven to be a fertile model system with which to identify glucose signaling factors, determine the relevant functional and physical interrelationships, and characterize the corresponding metabolic, transcriptomic, and proteomic readouts. The early events in glucose signaling appear to require both extracellular sensing by transmembrane proteins and i

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Lengeler, Klaus B., Robert C. Davidson, Cletus D'souza, et al. "Signal Transduction Cascades Regulating Fungal Development and Virulence." Microbiology and Molecular Biology Reviews 64, no. 4 (2000): 746–85. http://dx.doi.org/10.1128/mmbr.64.4.746-785.2000.

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SUMMARY Cellular differentiation, mating, and filamentous growth are regulated in many fungi by environmental and nutritional signals. For example, in response to nitrogen limitation, diploid cells of the yeast Saccharomyces cerevisiae undergo a dimorphic transition to filamentous growth referred to as pseudohyphal differentiation. Yeast filamentous growth is regulated, in part, by two conserved signal transduction cascades: a mitogen-activated protein kinase cascade and a G-protein regulated cyclic AMP signaling pathway. Related signaling cascades play an analogous role in regulating mating a

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Xu, Gang, Gregor Jansen, David Y. Thomas, Cornelis P. Hollenberg, and Massoud Ramezani Rad. "Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae." Molecular Microbiology 20, no. 4 (1996): 773–83. http://dx.doi.org/10.1111/j.1365-2958.1996.tb02516.x.

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BROACH, J. "RAS genes in Saccharomyces cerevisiae: signal transduction in search of a pathway." Trends in Genetics 7, no. 1 (1991): 28–33. http://dx.doi.org/10.1016/0168-9525(91)90018-l.

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Loomis, W. F., G. Shaulsky, and N. Wang. "Histidine kinases in signal transduction pathways of eukaryotes." Journal of Cell Science 110, no. 10 (1997): 1141–45. http://dx.doi.org/10.1242/jcs.110.10.1141.

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Autophosphorylating histidine kinases are an ancient conserved family of enzymes that are found in eubacteria, archaebacteria and eukaryotes. They are activated by a wide range of extracellular signals and transfer phosphate moieties to aspartates found in response regulators. Recent studies have shown that such two-component signal transduction pathways mediate osmoregulation in Saccharomyces cerevisiae, Dictyostelium discoideum and Neurospora crassa. Moreover, they play pivotal roles in responses of Arabidopsis thaliana to ethylene and cytokinin. A transmembrane histidine kinase encoded by d

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Alepuz, Paula M., Dina Matheos, Kyle W. Cunningham, and Francisco Estruch. "The Saccharomyces cerevisiae RanGTP-Binding Protein Msn5p Is Involved in Different Signal Transduction Pathways." Genetics 153, no. 3 (1999): 1219–31. http://dx.doi.org/10.1093/genetics/153.3.1219.

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Abstract In eukaryotes, control of transcription by extracellular signals involves the translocation to the nucleus of at least one component of the signal transduction pathway. Transport through the nuclear envelope requires the activity of an import or export receptor that interacts with the small GTPase Ran. We have cloned the MSN5 gene of the yeast Saccharomyces cerevisiae that is postulated to encode one of these receptors. Msn5p belongs to a family of proteins with a conserved N-terminal sequence that acts as a RanGTP-binding domain. The results presented here provide genetic data suppor

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Gomez, Shawn M., Shaw-Hwa Lo, and Andrey Rzhetsky. "Probabilistic Prediction of Unknown Metabolic and Signal-Transduction Networks." Genetics 159, no. 3 (2001): 1291–98. http://dx.doi.org/10.1093/genetics/159.3.1291.

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Abstract Regulatory networks provide control over complex cell behavior in all kingdoms of life. Here we describe a statistical model, based on representing proteins as collections of domains or motifs, which predicts unknown molecular interactions within these biological networks. Using known protein-protein interactions of Saccharomyces cerevisiae as training data, we were able to predict the links within this network with only 7% false-negative and 10% false-positive error rates. We also use Markov chain Monte Carlo simulation for the prediction of networks with maximum probability under ou

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Brill, J. A., E. A. Elion, and G. R. Fink. "A role for autophosphorylation revealed by activated alleles of FUS3, the yeast MAP kinase homolog." Molecular Biology of the Cell 5, no. 3 (1994): 297–312. http://dx.doi.org/10.1091/mbc.5.3.297.

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We have isolated dominant gain-of-function (gf) mutations in FUS3, a Saccharomyces cerevisiae mitogen-activated protein (MAP) kinase homolog, that constitutively activate the yeast mating signal transduction pathway and confer hypersensitivity to mating pheromone. Surprisingly, the phenotypes of dominant FUS3gf mutations require the two protein kinases, STE7 and STE11. FUS3gf kinases are hyperphosphorylated in yeast independently of STE7. Consistent with this, FUS3gf kinases expressed in Escherichia coli exhibit an increased ability to autophosphorylate on tyrosine in vivo. FUS3gf mutations su

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Levin, David E. "Cell Wall Integrity Signaling in Saccharomyces cerevisiae." Microbiology and Molecular Biology Reviews 69, no. 2 (2005): 262–91. http://dx.doi.org/10.1128/mmbr.69.2.262-291.2005.

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SUMMARY The yeast cell wall is a highly dynamic structure that is responsible for protecting the cell from rapid changes in external osmotic potential. The wall is also critical for cell expansion during growth and morphogenesis. This review discusses recent advances in understanding the various signal transduction pathways that allow cells to monitor the state of the cell wall and respond to environmental challenges to this structure. The cell wall integrity signaling pathway controlled by the small G-protein Rho1 is principally responsible for orchestrating changes to the cell wall periodica

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Lu, Jade Mei-Yeh, Robert J. Deschenes, and Jan S. Fassler. "Role for the Ran Binding Protein, Mog1p, in Saccharomyces cerevisiae SLN1-SKN7 Signal Transduction." Eukaryotic Cell 3, no. 6 (2004): 1544–56. http://dx.doi.org/10.1128/ec.3.6.1544-1556.2004.

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ABSTRACT Yeast Sln1p is an osmotic stress sensor with histidine kinase activity. Modulation of Sln1 kinase activity in response to changes in the osmotic environment regulates the activity of the osmotic response mitogen-activated protein kinase pathway and the activity of the Skn7p transcription factor, both important for adaptation to changing osmotic stress conditions. Many aspects of Sln1 function, such as how kinase activity is regulated to allow a rapid response to the continually changing osmotic environment, are not understood. To gain insight into Sln1p function, we conducted a two-hy

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Cole, G. M., D. E. Stone, and S. I. Reed. "Stoichiometry of G protein subunits affects the Saccharomyces cerevisiae mating pheromone signal transduction pathway." Molecular and Cellular Biology 10, no. 2 (1990): 510–17. http://dx.doi.org/10.1128/mcb.10.2.510.

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The Saccharomyces cerevisiae GPA1, STE4, and STE18 genes encode products homologous to mammalian G-protein alpha, beta, and gamma subunits, respectively. All three genes function in the transduction of the signal generated by mating pheromone in haploid cells. To characterize more completely the role of these genes in mating, we have conditionally overexpressed GPA1, STE4, and STE18, using the galactose-inducible GAL1 promoter. Overexpression of STE4 alone, or STE4 together with STE18, generated a response in haploid cells suggestive of pheromone signal transduction: arrest in G1 of the cell c

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Cole, G. M., D. E. Stone, and S. I. Reed. "Stoichiometry of G protein subunits affects the Saccharomyces cerevisiae mating pheromone signal transduction pathway." Molecular and Cellular Biology 10, no. 2 (1990): 510–17. http://dx.doi.org/10.1128/mcb.10.2.510-517.1990.

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The Saccharomyces cerevisiae GPA1, STE4, and STE18 genes encode products homologous to mammalian G-protein alpha, beta, and gamma subunits, respectively. All three genes function in the transduction of the signal generated by mating pheromone in haploid cells. To characterize more completely the role of these genes in mating, we have conditionally overexpressed GPA1, STE4, and STE18, using the galactose-inducible GAL1 promoter. Overexpression of STE4 alone, or STE4 together with STE18, generated a response in haploid cells suggestive of pheromone signal transduction: arrest in G1 of the cell c

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Costa, V. "Oxidative stress and signal transduction in Saccharomyces cerevisiae: insights into ageing, apoptosis and diseases." Molecular Aspects of Medicine 22, no. 4-5 (2001): 217–46. http://dx.doi.org/10.1016/s0098-2997(01)00012-7.

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Gartner, A., K. Nasmyth, and G. Ammerer. "Signal transduction in Saccharomyces cerevisiae requires tyrosine and threonine phosphorylation of FUS3 and KSS1." Genes & Development 6, no. 7 (1992): 1280–92. http://dx.doi.org/10.1101/gad.6.7.1280.

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Vaseghi, Sam, Franz Macherhammer, Susanne Zibek, and Matthias Reuss. "Signal Transduction Dynamics of the Protein Kinase-A/Phosphofructokinase-2 System in Saccharomyces cerevisiae." Metabolic Engineering 3, no. 2 (2001): 163–72. http://dx.doi.org/10.1006/mben.2000.0179.

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Sitcheran, Raquel, Roger Emter, Anastasia Kralli, and Keith R. Yamamoto. "A Genetic Analysis of Glucocorticoid Receptor Signaling: Identification and Characterization of Ligand-Effect Modulators in Saccharomyces cerevisiae." Genetics 156, no. 3 (2000): 963–72. http://dx.doi.org/10.1093/genetics/156.3.963.

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Abstract To find novel components in the glucocorticoid signal transduction pathway, we performed a yeast genetic screen to identify ligand-effect modulators (LEMs), proteins that modulate the cellular response to hormone. We isolated several mutants that conferred increased glucocorticoid receptor (GR) activity in response to dexamethasone and analyzed two of them in detail. These studies identify two genes, LEM3 and LEM4, which correspond to YNL323w and ERG6, respectively. LEM3 is a putative transmembrane protein of unknown function, and ERG6 is a methyltransferase in the ergosterol biosynth

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Johnston, M., and J. H. Kim. "Glucose as a hormone: receptor-mediated glucose sensing in the yeast Saccharomyces cerevisiae." Biochemical Society Transactions 33, no. 1 (2005): 247–52. http://dx.doi.org/10.1042/bst0330247.

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Because glucose is the principal carbon and energy source for most cells, most organisms have evolved numerous and sophisticated mechanisms for sensing glucose and responding to it appropriately. This is especially apparent in the yeast Saccharomyces cerevisiae, where these regulatory mechanisms determine the distinctive fermentative metabolism of yeast, a lifestyle it shares with many kinds of tumour cells. Because energy generation by fermentation of glucose is inefficient, yeast cells must vigorously metabolize glucose. They do this, in part, by carefully regulating the first, rate-limiting

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Lau, W.-T. Walter, Ken R. Schneider, and Erin K. O’Shea. "A Genetic Study of Signaling Processes for Repression of PHO5 Transcription in Saccharomyces cerevisiae." Genetics 150, no. 4 (1998): 1349–59. http://dx.doi.org/10.1093/genetics/150.4.1349.

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Abstract In the yeast Saccharomyces cerevisiae, transcription of a secreted acid phosphatase, PHO5, is repressed in response to high concentrations of extracellular inorganic phosphate. To investigate the signal transduction pathway leading to transcriptional regulation of PHO5, we carried out a genetic selection for mutants that express PHO5 constitutively. We then screened for mutants whose phenotypes are also dependent on the function of PHO81, which encodes an inhibitor of the Pho80p-Pho85p cyclin/cyclin-dependent kinase complex. These mutations are therefore likely to impair upstream func

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Kim, Jeong-Ho, Valérie Brachet, Hisao Moriya, and Mark Johnston. "Integration of Transcriptional and Posttranslational Regulation in a Glucose Signal Transduction Pathway in Saccharomyces cerevisiae." Eukaryotic Cell 5, no. 1 (2006): 167–73. http://dx.doi.org/10.1128/ec.5.1.167-173.2006.

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ABSTRACT Expression of the HXT genes encoding glucose transporters in the budding yeast Saccharomyces cerevisiae is regulated by two interconnected glucose-signaling pathways: the Snf3/Rgt2-Rgt1 glucose induction pathway and the Snf1-Mig1 glucose repression pathway. The Snf3 and Rgt2 glucose sensors in the membrane generate a signal in the presence of glucose that inhibits the functions of Std1 and Mth1, paralogous proteins that regulate the function of the Rgt1 transcription factor, which binds to the HXT promoters. It is well established that glucose induces degradation of Mth1, but the fate

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Whiteway, M., L. Hougan, D. Dignard, et al. "Function of the STE4 and STE18 Genes in Mating Pheromone Signal Transduction in Saccharomyces cerevisiae." Cold Spring Harbor Symposia on Quantitative Biology 53 (January 1, 1988): 585–90. http://dx.doi.org/10.1101/sqb.1988.053.01.067.

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Nishimura, Hiroshi, Yuko Kawasaki, Kazuto Nosaka, and Yoshinobu Kaneko. "Mutation thi81 causing a deficiency in the signal transduction of thiamine pyrophosphate in Saccharomyces cerevisiae." FEMS Microbiology Letters 156, no. 2 (2006): 245–49. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12735.x.

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Suzuki-Fujimoto, T., M. Fukuma, K. I. Yano, et al. "Analysis of the galactose signal transduction pathway in Saccharomyces cerevisiae: interaction between Gal3p and Gal80p." Molecular and Cellular Biology 16, no. 5 (1996): 2504–8. http://dx.doi.org/10.1128/mcb.16.5.2504.

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The GAL3 gene plays a critical role in galactose induction of the GAL genes that encode galactose- metabolizing enzymes in Saccharomyces cerevisiae. Defects in GAL3 result in a long delay in GAL gene induction, and overproduction of Gal3p causes constitutive expression of GAL. Here we demonstrate that concomitant overproduction of the negative regulator, Gal80p, and Gal3p suppresses this constitutive GAL expression. This interplay between Gal80p and Gal3p is direct, as tagged Gal3p coimmunoprecipitated with Gal80p. The amount of coprecipitated Gal80p increased when GAL80 yeast cells were grown

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Liang, H., and R. F. Gaber. "A novel signal transduction pathway in Saccharomyces cerevisiae defined by Snf3-regulated expression of HXT6." Molecular Biology of the Cell 7, no. 12 (1996): 1953–66. http://dx.doi.org/10.1091/mbc.7.12.1953.

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We show that cells deleted for SNF3, HXT1, HXT2, HXT3, HXT4, HXT6, and HXT7 do not take up glucose and cannot grow on media containing glucose as a sole carbon source. The expression of Hxt1, Hxt2, Hxt3, Hxt6, or Gal2 in these cells resulted in glucose transport and allowed growth on glucose media. In contrast, the expression of Snf3 failed to confer glucose uptake or growth on glucose. HXT6 is highly expressed on raffinose, low glucose, or nonfermentable carbon sources but is repressed in the presence of high concentrations of glucose. The maintenance of HXT6 glucose repression is strictly de

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Zhou, Z., A. Gartner, R. Cade, G. Ammerer, and B. Errede. "Pheromone-induced signal transduction in Saccharomyces cerevisiae requires the sequential function of three protein kinases." Molecular and Cellular Biology 13, no. 4 (1993): 2069–80. http://dx.doi.org/10.1128/mcb.13.4.2069.

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Protein phosphorylation plays an important role in pheromone-induced differentiation processes of haploid yeast cells. Among the components necessary for signal transduction are the STE7 and STE11 kinases and either one of the redundant FUS3 and KSS1 kinases. FUS3 and presumably KSS1 are phosphorylated and activated during pheromone induction by a STE7-dependent mechanism. Pheromone also induces the accumulation of STE7 in a hyperphosphorylated form. This modification of STE7 requires the STE11 kinase, which is proposed to act before STE7 during signal transmission. Surprisingly, STE7 hyperpho

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Bhat, P. J., D. Oh, and J. E. Hopper. "Analysis of the GAL3 signal transduction pathway activating GAL4 protein-dependent transcription in Saccharomyces cerevisiae." Genetics 125, no. 2 (1990): 281–91. http://dx.doi.org/10.1093/genetics/125.2.281.

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Abstract The Saccharomyces cerevisiae GAL/MEL regulon genes are normally induced within minutes of galactose addition, but gal3 mutants exhibit a 3-5-day induction lag. We have discovered that this long-term adaptation (LTA) phenotype conferred by gal3 is complemented by multiple copies of the GAL1 gene. Based on this result and the striking similarity between the GAL3 and GAL1 protein sequences we attempted to detect galactokinase activity that might be associated with the GAL3 protein. By both in vivo and in vitro tests the GAL3 gene product does not appear to catalyze a galactokinase-like r

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Zhou, Z., A. Gartner, R. Cade, G. Ammerer, and B. Errede. "Pheromone-induced signal transduction in Saccharomyces cerevisiae requires the sequential function of three protein kinases." Molecular and Cellular Biology 13, no. 4 (1993): 2069–80. http://dx.doi.org/10.1128/mcb.13.4.2069-2080.1993.

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Protein phosphorylation plays an important role in pheromone-induced differentiation processes of haploid yeast cells. Among the components necessary for signal transduction are the STE7 and STE11 kinases and either one of the redundant FUS3 and KSS1 kinases. FUS3 and presumably KSS1 are phosphorylated and activated during pheromone induction by a STE7-dependent mechanism. Pheromone also induces the accumulation of STE7 in a hyperphosphorylated form. This modification of STE7 requires the STE11 kinase, which is proposed to act before STE7 during signal transmission. Surprisingly, STE7 hyperpho

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Holley, S. J., and K. R. Yamamoto. "A role for Hsp90 in retinoid receptor signal transduction." Molecular Biology of the Cell 6, no. 12 (1995): 1833–42. http://dx.doi.org/10.1091/mbc.6.12.1833.

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The ubiquitous heat shock protein Hsp90 appears to participate directly in the function of a broad range of cellular signal transduction components, including steroid hormone receptors; however, an evolutionarily related subclass of intracellular receptors, exemplified by the retinoid receptors RAR and RXR, had been inferred from biochemical studies to function independently of Hsp90. To examine this issue genetically, we measured mammalian and avian retinoid receptor activity in a Saccharomyces cerevisiae strain in which the expression of the yeast Hsp90 homologue could be conditionally repre

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Whiteway, Malcolm, Daniel Dignard та David Y. Thomas. "Mutagenesis of Ste18, a putative Gγ subunit in the Saccharomyces cerevisiae pheromone response pathway". Biochemistry and Cell Biology 70, № 10-11 (1992): 1230–37. http://dx.doi.org/10.1139/o92-169.

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The yeast STE18 gene product has sequence and functional similarity to the γ subunits of G proteins. The cloned STE18 gene was subjected to a saturation mutagenesis using doped oligonucleotides. The populations of mutant genes were screened for two classes of STE18 mutations, those that allowed for increased mating of a strain containing a defective STE4 gene (compensators) and those that inhibited mating even in the presence of a functional STE18 gene (dominant negatives). Three amino acid substitutions that enhanced mating in a specific STE4 (Gβ) point mutant background were identified. Thes

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Cutler, N. Shane, Xuewen Pan, Joseph Heitman, and Maria E. Cardenas. "The TOR Signal Transduction Cascade Controls Cellular Differentiation in Response to Nutrients." Molecular Biology of the Cell 12, no. 12 (2001): 4103–13. http://dx.doi.org/10.1091/mbc.12.12.4103.

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Rapamycin binds and inhibits the Tor protein kinases, which function in a nutrient-sensing signal transduction pathway that has been conserved from the yeast Saccharomyces cerevisiaeto humans. In yeast cells, the Tor pathway has been implicated in regulating cellular responses to nutrients, including proliferation, translation, transcription, autophagy, and ribosome biogenesis. We report here that rapamycin inhibits pseudohyphal filamentous differentiation of S. cerevisiae in response to nitrogen limitation. Overexpression of Tap42, a protein phosphatase regulatory subunit, restored pseudohyph

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Gerst, J. E., K. Ferguson, A. Vojtek, M. Wigler, and J. Field. "CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex." Molecular and Cellular Biology 11, no. 3 (1991): 1248–57. http://dx.doi.org/10.1128/mcb.11.3.1248.

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CAP, a protein from Saccharomyces cerevisiae that copurifies with adenylyl cyclase, appears to be required for yeast cells to be fully responsive to RAS proteins. CAP also appears to be required for normal cell morphology and responsiveness to nutrient deprivation and excess. We describe here a molecular and phenotypic analysis of the CAP protein. The N-terminal domain is necessary and sufficient for cellular response to activated RAS protein, while the C-terminal domain is necessary and sufficient for normal cellular morphology and responses to nutrient extremes. Thus, CAP is a novel example

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Gerst, J. E., K. Ferguson, A. Vojtek, M. Wigler, and J. Field. "CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex." Molecular and Cellular Biology 11, no. 3 (1991): 1248–57. http://dx.doi.org/10.1128/mcb.11.3.1248-1257.1991.

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CAP, a protein from Saccharomyces cerevisiae that copurifies with adenylyl cyclase, appears to be required for yeast cells to be fully responsive to RAS proteins. CAP also appears to be required for normal cell morphology and responsiveness to nutrient deprivation and excess. We describe here a molecular and phenotypic analysis of the CAP protein. The N-terminal domain is necessary and sufficient for cellular response to activated RAS protein, while the C-terminal domain is necessary and sufficient for normal cellular morphology and responses to nutrient extremes. Thus, CAP is a novel example

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Yashar, B., K. Irie, J. A. Printen, et al. "Yeast MEK-dependent signal transduction: response thresholds and parameters affecting fidelity." Molecular and Cellular Biology 15, no. 12 (1995): 6545–53. http://dx.doi.org/10.1128/mcb.15.12.6545.

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Ste7p and Mkk1p are MEK (MAPK/ERK kinase) family members that function in the mating and cell integrity signal transduction pathways in Saccharomyces cerevisiae. We selected STE7 and MKK1 mutations that stimulated their respective pathways in the absence of an inductive signal. Strikingly, serine-to-proline substitutions at analogous positions in Ste7p (position 368) and Mkk1p (position 386) were recovered by independent genetic screens. Such an outcome suggests that this substitution in other MEKs would exhibit similar properties. The Ste7p-P368 variant has higher basal enzymatic activity tha

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Neiman, A. M., B. J. Stevenson, H. P. Xu, et al. "Functional homology of protein kinases required for sexual differentiation in Schizosaccharomyces pombe and Saccharomyces cerevisiae suggests a conserved signal transduction module in eukaryotic organisms." Molecular Biology of the Cell 4, no. 1 (1993): 107–20. http://dx.doi.org/10.1091/mbc.4.1.107.

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We present genetic evidence that three presumptive protein kinases of Schizosaccharomyces pombe, byr2, byr1, and spk1 that are structurally related to protein kinases of Saccharomyces cerevisiae, STE11, STE7, and FUS3, respectively, are also functionally related. In some cases, introduction of the heterologous protein kinase into a mutant was sufficient for complementation. In other cases (as in a ste11- mutant of S. cerevisiae), expression of two S. pombe protein kinases (byr2 and byr1) was required to observe complementation, suggesting that byr2 and byr1 act cooperatively. Complementation i

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Fujimura, H. A. "The yeast G-protein homolog is involved in the mating pheromone signal transduction system." Molecular and Cellular Biology 9, no. 1 (1989): 152–58. http://dx.doi.org/10.1128/mcb.9.1.152.

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I have isolated a new type of sterile mutant of Saccharomyces cerevisiae, carrying a single mutant allele, designated dac1, which was mapped near the centromere on chromosome VIII. The dac1 mutation caused specific defects in the pheromone responsiveness of both a and alpha cells and did not seem to be associated with any pleiotropic phenotypes. Thus, in contrast to the ste4, ste5, ste7, ste11, and ste12 mutations, the dac1 mutation had no significant effect on such constitutive functions of haploid cells as pheromone production and alpha-factor destruction. The characteristics of this phenoty

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Fujimura, H. A. "The yeast G-protein homolog is involved in the mating pheromone signal transduction system." Molecular and Cellular Biology 9, no. 1 (1989): 152–58. http://dx.doi.org/10.1128/mcb.9.1.152-158.1989.

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I have isolated a new type of sterile mutant of Saccharomyces cerevisiae, carrying a single mutant allele, designated dac1, which was mapped near the centromere on chromosome VIII. The dac1 mutation caused specific defects in the pheromone responsiveness of both a and alpha cells and did not seem to be associated with any pleiotropic phenotypes. Thus, in contrast to the ste4, ste5, ste7, ste11, and ste12 mutations, the dac1 mutation had no significant effect on such constitutive functions of haploid cells as pheromone production and alpha-factor destruction. The characteristics of this phenoty

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Henry, Theresa C., Juliette E. Power, Christine L. Kerwin, et al. "Systematic Screen of Schizosaccharomyces pombe Deletion Collection Uncovers Parallel Evolution of the Phosphate Signal Transduction Pathway in Yeasts." Eukaryotic Cell 10, no. 2 (2010): 198–206. http://dx.doi.org/10.1128/ec.00216-10.

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ABSTRACT The phosphate signal transduction (PHO) pathway, which regulates genes in response to phosphate starvation, is well defined in Saccharomyces cerevisiae . We asked whether the PHO pathway was the same in the distantly related fission yeast Schizosaccharomyces pombe . We screened a deletion collection for mutants aberrant in phosphatase activity, which is primarily a consequence of pho1 + transcription. We identified a novel zinc finger-containing protein (encoded by spbc27b12.11c + ), which we have named pho7 + , that is essential for pho1 + transcriptional induction during phosphate s

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Horecka, Joe, and George F. Sprague. "Identification and Characterization of FAR3, a Gene Required for Pheromone-Mediated G1 Arrest in Saccharomyces cerevisiae." Genetics 144, no. 3 (1996): 905–21. http://dx.doi.org/10.1093/genetics/144.3.905.

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Abstract In haploid Saccharomyces cerevisiae cells, mating pheromones activate a signal transduction pathway that leads to cell cycle arrest in the G1 phase and to transcription induction of genes that promote conjugation. To identify genes that link the signal transduction pathway and the cell cycle machinery, we developed a selection strategy to isolate yeast mutants specifically defective for G1 arrest. Several of these mutants identified previously known genes, including CLN3, FUS3, and FAR1. In addition, a new gene, FAR3, was identified and characterized. FAR3 encodes a novel protein of 2

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Styrkársdóttir, Unnur, Richard Egel, and Olaf Nielsen. "Functional conservation between Schizosaccharomyces pombe ste8 and Saccharomyces cerevisiae STE11 protein kinases in yeast signal transduction." Molecular and General Genetics MGG 235, no. 1 (1992): 122–30. http://dx.doi.org/10.1007/bf00286189.

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Sadhu, C., D. Hoekstra, M. J. McEachern, S. I. Reed, and J. B. Hicks. "A G-protein alpha subunit from asexual Candida albicans functions in the mating signal transduction pathway of Saccharomyces cerevisiae and is regulated by the a1-alpha 2 repressor." Molecular and Cellular Biology 12, no. 5 (1992): 1977–85. http://dx.doi.org/10.1128/mcb.12.5.1977.

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We have isolated a gene, designated CAG1, from Candida albicans by using the G-protein alpha-subunit clone SCG1 of Saccharomyces cerevisiae as a probe. Amino acid sequence comparison revealed that CAG1 is more homologous to SCG1 than to any other G protein reported so far. Homology between CAG1 and SCG1 not only includes the conserved guanine nucleotide binding domains but also spans the normally variable regions which are thought to be involved in interaction with the components of the specific signal transduction pathway. Furthermore, CAG1 contains a central domain, previously found only in

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Sadhu, C., D. Hoekstra, M. J. McEachern, S. I. Reed, and J. B. Hicks. "A G-protein alpha subunit from asexual Candida albicans functions in the mating signal transduction pathway of Saccharomyces cerevisiae and is regulated by the a1-alpha 2 repressor." Molecular and Cellular Biology 12, no. 5 (1992): 1977–85. http://dx.doi.org/10.1128/mcb.12.5.1977-1985.1992.

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We have isolated a gene, designated CAG1, from Candida albicans by using the G-protein alpha-subunit clone SCG1 of Saccharomyces cerevisiae as a probe. Amino acid sequence comparison revealed that CAG1 is more homologous to SCG1 than to any other G protein reported so far. Homology between CAG1 and SCG1 not only includes the conserved guanine nucleotide binding domains but also spans the normally variable regions which are thought to be involved in interaction with the components of the specific signal transduction pathway. Furthermore, CAG1 contains a central domain, previously found only in

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Biswas, Subhrajit, Patrick Van Dijck, and Asis Datta. "Environmental Sensing and Signal Transduction Pathways Regulating Morphopathogenic Determinants of Candida albicans." Microbiology and Molecular Biology Reviews 71, no. 2 (2007): 348–76. http://dx.doi.org/10.1128/mmbr.00009-06.

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SUMMARY Candida albicans is an opportunistic fungal pathogen that is found in the normal gastrointestinal flora of most healthy humans. However, under certain environmental conditions, it can become a life-threatening pathogen. The shift from commensal organism to pathogen is often correlated with the capacity to undergo morphogenesis. Indeed, under certain conditions, including growth at ambient temperature, the presence of serum or N-acetylglucosamine, neutral pH, and nutrient starvation, C. albicans can undergo reversible transitions from the yeast form to the mycelial form. This morphologi

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CHEN, AIMIN, JIAJUN ZHANG, ZHANJIANG YUAN, and TIANSHOU ZHOU. "NOISE-INDUCED ALTERNATIVE RESPONSE IN MAP KINASE PATHWAYS WITH MUTUAL INHIBITION." Journal of Biological Systems 17, no. 01 (2009): 125–40. http://dx.doi.org/10.1142/s021833900900282x.

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All organisms have the ability to detect and respond to changes in the environment for survival, and as a result, specific cellular signaling pathways have evolved by which organisms sense their environment and respond to signals that they detect. However, an important unsolved problem in cell biology is to understand how specificity from signal to cellular response is maintained between different signal transduction pathways that share similar or identical components. Here, we show, using mathematical and computational modeling, that two typical signaling pathways in a single cell, hyperosmol

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Schrick, Kathrin, Barbara Garvik, and Leland H. Hartwell. "Mating in Saccharomyces cerevisiae: The Role of the Pheromone Signal Transduction Pathway in the Chemotropic Response to Pheromone." Genetics 147, no. 1 (1997): 19–32. http://dx.doi.org/10.1093/genetics/147.1.19.

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Abstract The mating process in yeast has two distinct aspects. One is the induction and activation of proteins required for cell fusion in response to a pheromone signal; the other is chemotropism, i.e., detection of a pheromone gradient and construction of a fusion site available to the signaling cell. To determine whether components of the signal transduction pathway necessary for transcriptional activation also play a role in chemotropism, we examined strains with null mutations in components of the signal transduction pathway for diploid formation, prezygote formation and the chemotropic p

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