scholarly journals Function of the ste signal transduction pathway for mating pheromones sustains MAT alpha 1 transcription in Saccharomyces cerevisiae.

1993 ◽  
Vol 13 (4) ◽  
pp. 2050-2060 ◽  
Author(s):  
Y Mukai ◽  
S Harashima ◽  
Y Oshima
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signal Transduction ◽  
Signal Transduction Pathway ◽  
Single Copy ◽  
Upstream Region ◽  
Transduction Pathway ◽  
Mating Ability ◽  
Mating Pheromones ◽  
C Terminus ◽  
Dependent Protein

Sterile mutants of Saccharomyces cerevisiae were isolated from alpha * cells having the a/alpha aar1-6 genotype (exhibiting alpha mating ability and weak a mating ability as a result of a defect in a1-alpha 2 repression). Among these sterile mutants, we found two ste5 mutants together with putative ste7, ste11, and ste12 mutants of the signal transduction pathway of mating pheromones. The amino acid sequence of the Ste5p protein predicted from the nucleotide sequence of a cloned STE5 DNA has a domain rich in acidic amino acids close to its C terminus, a cysteine-rich sequence, resembling part of a zinc finger structure, in its N-terminal half, and a possible target site of cyclic AMP-dependent protein kinase at its C terminus. Northern (RNA) blot analysis revealed that STE5 transcription is under a1-alpha 2-Aar1p repression. The MAT alpha 1 cistron has a single copy of the pheromone response element in its 5' upstream region, and its basal level of transcription was reduced in these ste mutant cells. However, expression of the MAT alpha 1 cistron was not enhanced appreciably by pheromone signals. One of the ste5 mutant alleles conferred a sterile phenotype to a/alpha aar1-6 cells but a mating ability to MATa cells.

Function of the ste signal transduction pathway for mating pheromones sustains MAT alpha 1 transcription in Saccharomyces cerevisiae

1993 ◽  
Vol 13 (4) ◽  
pp. 2050-2060
Author(s):  
Y Mukai ◽  
S Harashima ◽  
Y Oshima
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signal Transduction ◽  
Signal Transduction Pathway ◽  
Single Copy ◽  
Upstream Region ◽  
Transduction Pathway ◽  
Mating Ability ◽  
Mating Pheromones ◽  
C Terminus ◽  
Dependent Protein

Sterile mutants of Saccharomyces cerevisiae were isolated from alpha * cells having the a/alpha aar1-6 genotype (exhibiting alpha mating ability and weak a mating ability as a result of a defect in a1-alpha 2 repression). Among these sterile mutants, we found two ste5 mutants together with putative ste7, ste11, and ste12 mutants of the signal transduction pathway of mating pheromones. The amino acid sequence of the Ste5p protein predicted from the nucleotide sequence of a cloned STE5 DNA has a domain rich in acidic amino acids close to its C terminus, a cysteine-rich sequence, resembling part of a zinc finger structure, in its N-terminal half, and a possible target site of cyclic AMP-dependent protein kinase at its C terminus. Northern (RNA) blot analysis revealed that STE5 transcription is under a1-alpha 2-Aar1p repression. The MAT alpha 1 cistron has a single copy of the pheromone response element in its 5' upstream region, and its basal level of transcription was reduced in these ste mutant cells. However, expression of the MAT alpha 1 cistron was not enhanced appreciably by pheromone signals. One of the ste5 mutant alleles conferred a sterile phenotype to a/alpha aar1-6 cells but a mating ability to MATa cells.

Involvement of cyclic AMP-dependent protein kinases in the signal transduction pathway for interleukin-1

1990 ◽  
Vol 10 (7) ◽  
pp. 3824-3827
Author(s):  
M Chedid ◽  
S B Mizel
Keyword(s):  
Signal Transduction ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Gene Transcription ◽  
Interleukin 1 ◽  
Signal Transduction Pathway ◽  
Cell Types ◽  
Specific Protein ◽  
Transduction Pathway ◽  
Dependent Protein

Expression of a highly specific protein inhibitor for cyclic AMP-dependent protein kinases in interleukin-1 (IL-1)-responsive cells blocked IL-1-induced gene transcription that was driven by the kappa immunoglobulin enhancer or the human immunodeficiency virus long terminal repeat. This inhibitor did not affect protein kinase C-mediated gene transcription, suggesting that cyclic AMP-dependent protein kinases are involved in the signal transduction pathway for IL-1 in a number of responsive cell types.

Participation of cAMP in a signal-transduction pathway relating erythrocyte deformation to ATP release

2001 ◽  
Vol 281 (4) ◽  
pp. C1158-C1164 ◽  
Author(s):  
Randy S. Sprague ◽  
Mary L. Ellsworth ◽  
Alan H. Stephenson ◽  
Andrew J. Lonigro
Keyword(s):  
Signal Transduction ◽  
Adenylyl Cyclase ◽  
Atp Release ◽  
Signal Transduction Pathway ◽  
Intracellular Camp ◽  
Transmembrane Conductance Regulator ◽  
Transduction Pathway ◽  
Camp Analog ◽  
Dependent Protein ◽  
Erythrocyte Deformation

Previously, we reported that red blood cells (RBCs) of rabbits and humans release ATP in response to mechanical deformation and that this release of ATP requires the activity of the cystic fibrosis transmembrane conductance regulator (CFTR). It was reported that cAMP, acting through a cAMP-dependent protein kinase, PKA, is an activator of CFTR. Here we investigate the hypothesis that cAMP stimulates ATP release from RBCs. Incubation of human and rabbit RBCs with the direct activator of adenylyl cyclase, forskolin (10 or 100 μM), with IBMX (100 μM), resulted in ATP release and increases in intracellular cAMP. In addition, epinephrine (1 μM), a receptor-mediated activator of adenylyl cyclase, stimulated ATP release from rabbit RBCs. Moreover, incubation of human and rabbit RBCs with an active cAMP analog [adenosine 3′5′-cyclic monophosphorothioate Sp-isomer (Sp-cAMP, 100 μM)] resulted in ATP release. In contrast, forskolin and Sp-cAMP were without effect on dog RBCs, cells known not to release ATP in response to deformation. When rabbit RBCs were incubated with the inactive cAMP analog and inhibitor of PKA activity, adenosine 3′,5′-cyclic monophosphorothioate Rp-isomer (100 μM), deformation-induced ATP release was attenuated. These results are consistent with the hypothesis that adenylyl cyclase and cAMP are components of a signal-transduction pathway relating RBC deformation to ATP release from human and rabbit RBCs.

scholarly journals 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.

1992 ◽  
Vol 12 (5) ◽  
pp. 1977-1985 ◽  
Author(s):  
C Sadhu ◽  
D Hoekstra ◽  
M J McEachern ◽  
S I Reed ◽  
J B Hicks
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signal Transduction ◽  
Candida Albicans ◽  
G Protein ◽  
Signal Transduction Pathway ◽  
Alpha Subunit ◽  
Transduction Pathway ◽  
G Protein Alpha Subunit ◽  
Protein Alpha Subunit ◽  
Null Mutants

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 SCG1. cag1 null mutants of C. albicans created by gene disruption produced no readily detectable phenotype. The C. albicans CAG1 gene complemented both the growth and mating defects of S. cerevisiae scg1 null mutants when carried on either a low- or high-copy-number plasmid. In diploid C. albicans, the CAG1 transcript was readily detectable in mycelial and yeast cells of both the white and opaque forms. However, the CAG1-specific transcript in S. cerevisiae transformants containing the C. albicans CAG1 gene was observed only in haploid cells. This transcription pattern matches that of SCG1 in S. cerevisiae and is caused by a1-alpha 2 mediated repression in diploid cells. That is, CAG1 behaves as a haploid-specific gene in S. cerevisiae, subject to control by the a1-alpha 2 mating-type regulation pathway. We infer from these results that C. albicans may have a signal transduction system analogous to that controlling mating type in S. cerevisiae or possibly even a sexual pathway that has so far remained undetected.

scholarly journals A Genetic Study of Signaling Processes for Repression of PHO5 Transcription in Saccharomyces cerevisiae

Genetics ◽  
1998 ◽  
Vol 150 (4) ◽  
pp. 1349-1359 ◽  
Author(s):  
W-T Walter Lau ◽  
Ken R Schneider ◽  
Erin K O’Shea
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signal Transduction ◽  
Constitutive Expression ◽  
Signal Transduction Pathway ◽  
Acid Synthesis ◽  
Phosphate Transport ◽  
Transduction Pathway ◽  
Plasma Membrane Atpase ◽  
Yeast Saccharomyces Cerevisiae

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 functions in the signaling pathway, and they define five complementation groups. Mutations were found in a gene encoding a plasma membrane ATPase (PMA1), in genes required for the in vivo function of the phosphate transport system (PHO84 and PHO86), in a gene involved in the fatty acid synthesis pathway (ACC1), and in a novel, nonessential gene (PHO23). These mutants can be classified into two groups: pho84, pho86, and pma1 are defective in high-affinity phosphate uptake, whereas acc1 and pho23 are not, indicating that the two groups of mutations cause constitutive expression of PHO5 by distinct mechanisms. Our observations suggest that these gene products affect different aspects of the signal transduction pathway for PHO5 repression.

scholarly journals Wenxin-Keli Regulates the Calcium/Calmodulin-Dependent Protein Kinase II Signal Transduction Pathway and Inhibits Cardiac Arrhythmia in Rats with Myocardial Infarction

2013 ◽  
Vol 2013 ◽  
pp. 1-15 ◽  
Author(s):  
Yanwei Xing ◽  
Yonghong Gao ◽  
Jianxin Chen ◽  
Haiyan Zhu ◽  
Aiming Wu ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Heart Failure ◽  
Signal Transduction ◽  
Protein Kinase ◽  
Signal Transduction Pathway ◽  
Treated Group ◽  
Transduction Pathway ◽  
Dependent Protein Kinase ◽  
Group A ◽  
Dependent Protein

Wenxin-Keli (WXKL) is a Chinese herbal compound reported to be of benefit in the treatment of cardiac arrhythmia, cardiac inflammation, and heart failure. Amiodarone is a noncompetitive inhibitor of theα- andβ-adrenergic receptors and prevents calcium influx in the slow-response cells of the sinoatrial and atrioventricular nodes. Overexpression of Ca2+/calmodulin-dependent protein kinase II (CaMKII) in transgenic mice results in heart failure and arrhythmias. We hypothesised that administration of WXKL and amiodarone can reduce the incidence of arrhythmias by regulating CaMKII signal transduction. A total of 100 healthy Sprague Dawley rats were used in the study. The rats were randomly divided into four groups (a sham group, a myocardial infarction (MI) group, a WXKL-treated group, and an amiodarone-treated group). A myocardial infarction model was established in these rats by ligating the left anterior descending coronary artery for 4 weeks. Western blotting was used to assess CaMKII, p-CaMKII (Thr-286), PLB, p-PLB (Thr-17), RYR2, and FK binding protein 12.6 (FKBP12.6) levels. The Ca2+content in the sarcoplasmic reticulum (SR) and the calcium transient amplitude were studied by confocal imaging using the fluorescent indicator Fura-4. In conclusion, WXKL may inhibit heart failure and cardiac arrhythmias by regulating the CaMKII signal transduction pathway similar to amiodarone.

scholarly journals Involvement of cyclic AMP-dependent protein kinases in the signal transduction pathway for interleukin-1.

1990 ◽  
Vol 10 (7) ◽  
pp. 3824-3827 ◽  
Author(s):  
M Chedid ◽  
S B Mizel
Keyword(s):  
Signal Transduction ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Gene Transcription ◽  
Interleukin 1 ◽  
Signal Transduction Pathway ◽  
Cell Types ◽  
Specific Protein ◽  
Transduction Pathway ◽  
Dependent Protein

Expression of a highly specific protein inhibitor for cyclic AMP-dependent protein kinases in interleukin-1 (IL-1)-responsive cells blocked IL-1-induced gene transcription that was driven by the kappa immunoglobulin enhancer or the human immunodeficiency virus long terminal repeat. This inhibitor did not affect protein kinase C-mediated gene transcription, suggesting that cyclic AMP-dependent protein kinases are involved in the signal transduction pathway for IL-1 in a number of responsive cell types.

scholarly journals Isolation of Degradation-Deficient Mutants Defective in the Targeting of Fructose-1,6-bisphosphatase into the Vacuole for Degradation in Saccharomyces cerevisiae

Genetics ◽  
1996 ◽  
Vol 143 (4) ◽  
pp. 1555-1566 ◽  
Author(s):  
Mark Hoffman ◽  
Hui-Ling Chiang
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Signal Transduction ◽  
Carbon Source ◽  
Signal Transduction Pathway ◽  
Degradation Pathway ◽  
Transduction Pathway ◽  
Fructose 1,6 Bisphosphatase ◽  
Dependent Signal ◽  
Complementation Groups ◽  
Vacuolar Sorting

Abstract The key regulatory enzyme in the gluconeogenesis pathway, fructose-1,6-bisphosphatase (FBPase), is induced when Saccharomyces cerevisiae are grown in medium containing a poor carbon source. FBPase is targeted to the yeast vacuole for degradation when glucose-starved cells are replenished with fresh glucose. To identify genes involved in the FBPase degradation pathway, mutants that failed to degrade FBPase in response to glucose were isolated using a colony-blotting procedure. These vacuolar import and degradation-deficient (vid) mutants were placed into 20 complementation groups. They are distinct from the known sec, ups or pep mutants affecting protein secretion, vacuolar sorting and vacuolar proteolysis in that they sort CpY correctly and regulate osmotic pressure normally. Despite the presence of FBPase antigen in these mutants, FBPase is completely inactivated in all uid mutants, indicating that the c-AMP-dependent signal transduction pathway and inactivation must function properly in vid mutants. vid mutants block FBPase dzgradation by accumulating FBPase in the cytosol and also in small vesicles in the cytoplasm. FBPase may be targeted to small vesicles before uptake by the vacuole.

Sign in / Sign up

Export Citation Format

Share Document