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Journal articles on the topic 'Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Signal Transduction'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

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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2

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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3

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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4

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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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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6

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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7

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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9

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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10

Mösch, Hans-Ulrich, and Gerald R. Fink. "Dissection of Filamentous Growth by Transposon Mutagenesis in Saccharomyces cerevisiae." Genetics 145, no. 3 (1997): 671–84. http://dx.doi.org/10.1093/genetics/145.3.671.

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Diploid Saccharomyces cerevisiae strains starved for nitrogen undergo a developmental transition from growth as single yeast form (YF) cells to a multicellular form consisting of filaments of pseudohyphal (PH) cells. Filamentous growth is regulated by an evolutionarily conserved signaling pathway that includes the small GTP-binding proteins Ras2p and Cdc42p, the protein kinases Ste20p, Ste11p and Ste7p, and the transcription factor Ste12p. Here, we designed a genetic screen for mutant strains defective for filamentous growth (dfg) to identify novel targets of the filamentation signaling pathwa

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11

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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12

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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13

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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14

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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15

Miyajima, I., N. Nakayama, M. Nakafuku, Y. Kaziro, K. Arai, and K. Matsumoto. "Suppressors of a gpa1 mutation cause sterility in Saccharomyces cerevisiae." Genetics 119, no. 4 (1988): 797–804. http://dx.doi.org/10.1093/genetics/119.4.797.

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Abstract The Saccharomyces cerevisiae GPA1 gene encodes a protein highly homologous to the alpha subunit of mammalian G proteins and is essential for haploid cell growth. We have selected 77 mutants able to suppress the lethality resulting from disruption of GPA1 (gpa1::HIS3). Two strains bearing either of two recessive mutations, sgp1 and sgp2, in combination with the disruption mutation, showed a cell type nonspecific sterile phenotype, yet expressed the major alpha-factor gene (MF alpha 1) as judged by the ability to express a MF alpha 1-lacZ fusion gene. The sgp1 mutation was closely linke

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16

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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17

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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18

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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19

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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20

Barr, M. M., H. Tu, L. Van Aelst, and M. Wigler. "Identification of Ste4 as a potential regulator of Byr2 in the sexual response pathway of Schizosaccharomyces pombe." Molecular and Cellular Biology 16, no. 10 (1996): 5597–603. http://dx.doi.org/10.1128/mcb.16.10.5597.

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A conserved MAP kinase cascade is central to signal transduction in both simple and complex eukaryotes. In the yeast Schizosaccharomyces pombe, Byr2, a homolog of mammalian MAPK/ERK kinase kinase and Saccharomyces cerevisiae STE11, is required for pheromone-induced sexual differentiation. A screen for S. pombe proteins that interact with Byr2 in a two-hybrid system led to the isolation of Ste4, a protein that is known to be required for sexual function. Ste4 binds to the regulatory region of Byr2. This binding site is separable from the binding site for Ras1. Both Ste4 and Ras1 act upstream of

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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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24

Yoon, Je-Hyun, Eui-Ju Choi, and Roy Parker. "Dcp2 phosphorylation by Ste20 modulates stress granule assembly and mRNA decay in Saccharomyces cerevisiae." Journal of Cell Biology 189, no. 5 (2010): 813–27. http://dx.doi.org/10.1083/jcb.200912019.

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Translation and messenger RNA (mRNA) degradation are important sites of gene regulation, particularly during stress where translation and mRNA degradation are reprogrammed to stabilize bulk mRNAs and to preferentially translate mRNAs required for the stress response. During stress, untranslating mRNAs accumulate both in processing bodies (P-bodies), which contain some translation repressors and the mRNA degradation machinery, and in stress granules, which contain mRNAs stalled in translation initiation. How signal transduction pathways impinge on proteins modulating P-body and stress granule f

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25

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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26

Catlett, Natalie L., Olen C. Yoder, and B. Gillian Turgeon. "Whole-Genome Analysis of Two-Component Signal Transduction Genes in Fungal Pathogens." Eukaryotic Cell 2, no. 6 (2003): 1151–61. http://dx.doi.org/10.1128/ec.2.6.1151-1161.2003.

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ABSTRACT Two-component phosphorelay systems are minimally comprised of a histidine kinase (HK) component, which autophosphorylates in response to an environmental stimulus, and a response regulator (RR) component, which transmits the signal, resulting in an output such as activation of transcription, or of a mitogen-activated protein kinase cascade. The genomes of the yeasts Saccharomyces cerevisiae, Schizosaccharomyces pombe, and Candida albicans encode one, three, and three HKs, respectively. In contrast, the genome sequences of the filamentous ascomycetes Neurospora crassa, Cochliobolus het

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McBride, Anne E., Cecilia Zurita-Lopez, Anthony Regis, et al. "Protein Arginine Methylation in Candida albicans: Role in Nuclear Transport." Eukaryotic Cell 6, no. 7 (2007): 1119–29. http://dx.doi.org/10.1128/ec.00074-07.

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ABSTRACT Protein arginine methylation plays a key role in numerous eukaryotic processes, such as protein transport and signal transduction. In Candida albicans, two candidate protein arginine methyltransferases (PRMTs) have been identified from the genome sequencing project. Based on sequence comparison, C. albicans candidate PRMTs display similarity to Saccharomyces cerevisiae Hmt1 and Rmt2. Here we demonstrate functional homology of Hmt1 between C. albicans and S. cerevisiae: CaHmt1 supports growth of S. cerevisiae strains that require Hmt1, and CaHmt1 methylates Npl3, a major Hmt1 substrate

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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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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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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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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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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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Jethmalani, Yogita, and Erin M. Green. "Using Yeast to Define the Regulatory Role of Protein Lysine Methylation." Current Protein & Peptide Science 21, no. 7 (2020): 690–98. http://dx.doi.org/10.2174/1389203720666191023150727.

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The post-translational modifications (PTM) of proteins are crucial for cells to survive under diverse environmental conditions and to respond to stimuli. PTMs are known to govern a broad array of cellular processes including signal transduction and chromatin regulation. The PTM lysine methylation has been extensively studied within the context of chromatin and the epigenetic regulation of the genome. However, it has also emerged as a critical regulator of non-histone proteins important for signal transduction pathways. While the number of known non-histone protein methylation events is increas

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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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Schmidt, A., M. N. Hall, and A. Koller. "Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake." Molecular and Cellular Biology 14, no. 10 (1994): 6597–606. http://dx.doi.org/10.1128/mcb.14.10.6597.

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The macrocyclic lactone FK506 exerts immunosuppressive effects on T lymphocytes by interfering with signal transduction leading to T-cell activation and also inhibits the growth of eukaryotic microorganisms, including Saccharomyces cerevisiae. We reported previously that an FK506-sensitive target in S. cerevisiae is required for amino acid import and that overexpression of two new genes, TAT1 and TAT2 (formerly called TAP1 and TAP2), confers resistance to the drug. Here we report that TAT1 and TAT2 encode novel members of the yeast amino acid permease family composed of integral membrane prote

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Schmidt, A., M. N. Hall, and A. Koller. "Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2, encode amino acid permeases mediating tyrosine and tryptophan uptake." Molecular and Cellular Biology 14, no. 10 (1994): 6597–606. http://dx.doi.org/10.1128/mcb.14.10.6597-6606.1994.

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The macrocyclic lactone FK506 exerts immunosuppressive effects on T lymphocytes by interfering with signal transduction leading to T-cell activation and also inhibits the growth of eukaryotic microorganisms, including Saccharomyces cerevisiae. We reported previously that an FK506-sensitive target in S. cerevisiae is required for amino acid import and that overexpression of two new genes, TAT1 and TAT2 (formerly called TAP1 and TAP2), confers resistance to the drug. Here we report that TAT1 and TAT2 encode novel members of the yeast amino acid permease family composed of integral membrane prote

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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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Abeliovich, Hagai, William A. Dunn, John Kim, and Daniel J. Klionsky. "Dissection of Autophagosome Biogenesis into Distinct Nucleation and Expansion Steps." Journal of Cell Biology 151, no. 5 (2000): 1025–34. http://dx.doi.org/10.1083/jcb.151.5.1025.

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Rapamycin, an antifungal macrolide antibiotic, mimics starvation conditions in Saccharomyces cerevisiae through activation of a general G0 program that includes widespread effects on translation and transcription. Macroautophagy, a catabolic membrane trafficking phenomenon, is a prominent part of this response. Two views of the induction of autophagy may be considered. In one, up-regulation of proteins involved in autophagy causes its induction, implying that autophagy is the result of a signal transduction mechanism leading from Tor to the transcriptional and translational machinery. An alter

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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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Demczuk, Agnieszka, Nilanjan Guha, Peter H. Nguyen, et al. "Saccharomyces cerevisiae Phospholipase C Regulates Transcription of Msn2p-Dependent Stress-Responsive Genes." Eukaryotic Cell 7, no. 6 (2008): 967–79. http://dx.doi.org/10.1128/ec.00438-07.

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ABSTRACT Phosphatidylinositol phosphates are involved in signal transduction, cytoskeletal organization, and membrane trafficking. Inositol polyphosphates, produced from phosphatidylinositol phosphates by the phospholipase C-dependent pathway, regulate chromatin remodeling. We used genome-wide expression analysis to further investigate the roles of Plc1p (phosphoinositide-specific phospholipase C in Saccharomyces cerevisiae) and inositol polyphosphates in transcriptional regulation. Plc1p contributes to the regulation of approximately 2% of yeast genes in cells grown in rich medium. Most of th

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Blondel, Marc, Jean-Marc Galan, and Matthias Peter. "Isolation and Characterization of HRT1 Using a Genetic Screen for Mutants Unable to Degrade Gic2p in Saccharomyces cerevisiae." Genetics 155, no. 3 (2000): 1033–44. http://dx.doi.org/10.1093/genetics/155.3.1033.

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Abstract Skp1p-cullin-F-box (SCF) protein complexes are ubiquitin ligases required for degradation of many regulatory proteins involved in cell cycle progression, morphogenesis, and signal transduction. Using a genetic screen, we have isolated a novel allele of the HRT1/RBX1 gene in budding yeast (hrt1-C81Y). hrt1-C81Y mutant cells exhibited an aberrant morphology but were viable at all temperatures. The cells displayed multiple genetic interactions with mutations in known SCF components and were defective for the degradation of several SCF targets including Gic2p, Far1p, Sic1p, and Cln2p. In

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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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Elion, E. A., B. Satterberg, and J. E. Kranz. "FUS3 phosphorylates multiple components of the mating signal transduction cascade: evidence for STE12 and FAR1." Molecular Biology of the Cell 4, no. 5 (1993): 495–510. http://dx.doi.org/10.1091/mbc.4.5.495.

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The mitogen-activated protein (MAP) kinase homologue FUS3 mediates both transcription and G1 arrest in a pheromone-induced signal transduction cascade in Saccharomyces cerevisiae. We report an in vitro kinase assay for FUS3 and its use in identifying candidate substrates. The assay requires catalytically active FUS3 and pheromone induction. STE7, a MAP kinase kinase homologue, is needed for maximal activity. At least seven proteins that specifically associate with FUS3 are phosphorylated in the assay. Many of these substrates are physiologically relevant and are affected by in vivo levels of n

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Rodicio, Rosaura, Sabrina Koch, Hans-Peter Schmitz, and Jürgen J. Heinisch. "KlRHO1 and KlPKC1 are essential for cell integrity signalling in Kluyveromyces lactis." Microbiology 152, no. 9 (2006): 2635–49. http://dx.doi.org/10.1099/mic.0.29105-0.

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Cell integrity in yeasts is ensured by a rigid cell wall whose synthesis is triggered by a MAP kinase-mediated signal-transduction cascade. Upstream regulatory components of this pathway in Saccharomyces cerevisiae involve a single protein kinase C, which is regulated by interaction with the small GTPase Rho1. Here, two genes were isolated which encode these proteins from Kluyveromyces lactis (KlPKC1 and KlRHO1). Sequencing showed ORFs which encode proteins of 1161 and 208 amino acids, respectively. The deduced proteins shared 59 and 85 % overall amino acid identities, respectively, with their

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Traincard, F., E. Ponte, J. Pun, B. Coukell, and M. Veron. "Evidence for the presence of an NF-kappaB signal transduction system in Dictyostelium discoideum." Journal of Cell Science 112, no. 20 (1999): 3529–35. http://dx.doi.org/10.1242/jcs.112.20.3529.

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The Rel/NF-kappaB family of transcription factors and regulators has so far only been described in vertebrates and arthropods, where they mediate responses to many extracellular signals. No counterparts of genes coding for such proteins have been identified in the Caenorhabditis elegans genome and no NF-kappaB activity was found in Saccharomyces cerevisiae. We describe here the presence of an NF-kappaB transduction pathway in the lower eukaryote Dictyostelium discoideum. Using antibodies raised against components of the mammalian NF-kappaB pathway, we demonstrate in Dictyostelium cells extract

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Li, Fang, and Sean P. Palecek. "EAP1, a Candida albicans Gene Involved in Binding Human Epithelial Cells." Eukaryotic Cell 2, no. 6 (2003): 1266–73. http://dx.doi.org/10.1128/ec.2.6.1266-1273.2003.

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ABSTRACT Candida albicans adhesion to host tissues contributes to its virulence and adhesion to medical devices permits biofilm formation, but we know relatively little about the molecular mechanisms governing C. albicans adhesion to materials or mammalian cells. Saccharomyces cerevisiae provides an attractive model system for studying adhesion in yeast because of its well-characterized genetics and gene expression systems and the conservation of signal transduction pathways among the yeasts. In this study, we used a parallel plate flow chamber to screen and characterize attachment of a flo8Δ

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Holtzman, DA, S. Yang, and DG Drubin. "Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae." Journal of Cell Biology 122, no. 3 (1993): 635–44. http://dx.doi.org/10.1083/jcb.122.3.635.

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Abplp is a yeast cortical actin-binding protein that contains an SH3 domain similar to those found in signal transduction proteins that function at the membrane/cytoskeleton interface. Although no detectable phenotypes are associated with a disruption allele of ABP1, mutations that create a requirement for this protein have now been isolated in the previously identified gene SAC6 and in two new genes, SLA1 and SLA2. The SAC6 gene encodes yeast fimbrin, an actin filament-bundling protein. Null mutations in SLA1 and SLA2 cause temperature-sensitive growth defects. Sla1p contains three SH3 domain

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Arévalo-Rodríguez, Miguel, and Joseph Heitman. "Cyclophilin A Is Localized to the Nucleus and Controls Meiosis in Saccharomyces cerevisiae." Eukaryotic Cell 4, no. 1 (2005): 17–29. http://dx.doi.org/10.1128/ec.4.1.17-29.2005.

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ABSTRACT Cyclophilin A is conserved from yeast to humans and mediates the ability of cyclosporine to perturb signal transduction cascades via inhibition of calcineurin. Cyclophilin A also catalyzes cis-trans peptidyl-prolyl isomerization during protein folding or conformational changes; however, cyclophilin A is not essential in yeast or human cells, and the true biological functions of this highly conserved enzyme have remained enigmatic. In Saccharomyces cerevisiae, cyclophilin A becomes essential in cells compromised for the nuclear prolyl-isomerase Ess1, and cyclophilin A physically intera

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Xu, Wenjie, Frank J. Smith, Ryan Subaran, and Aaron P. Mitchell. "Multivesicular Body-ESCRT Components Function in pH Response Regulation inSaccharomyces cerevisiaeandCandida albicans." Molecular Biology of the Cell 15, no. 12 (2004): 5528–37. http://dx.doi.org/10.1091/mbc.e04-08-0666.

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The ESCRT-I, -II, and -III protein complexes function to create multivesicular bodies (MVBs) for sorting of proteins destined for the lysosome or vacuole. Prior studies with Saccharomyces cerevisiae have shown that the ESCRT-III protein Snf7p interacts with the MVB pathway protein Bro1p as well as its homolog Rim20p. Rim20p has no role in MVB formation, but functions in the Rim101p pH-response pathway; Rim20p interacts with transcription factor Rim101p and is required for the activation of Rim101p by C-terminal proteolytic cleavage. We report here that ESCRT-III proteins Snf7p and Vps20p as we

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