scholarly journals Expression of the Glyoxalase I Gene ofSaccharomyces cerevisiaeIs Regulated by High Osmolarity Glycerol Mitogen-activated Protein Kinase Pathway in Osmotic Stress Response

1998 ◽  
Vol 273 (5) ◽  
pp. 2977-2983 ◽  
Author(s):  
Yoshiharu Inoue ◽  
Yoshiyuki Tsujimoto ◽  
Akira Kimura
Keyword(s):  
Stress Response ◽  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Glyoxalase I ◽  
High Osmolarity ◽  
High Osmolarity Glycerol ◽  
Osmotic Stress Response ◽  
Mitogen Activated Protein ◽  
Kinase Pathway ◽  
I Gene

scholarly journals Evidence of a New Role for the High-Osmolarity Glycerol Mitogen-Activated Protein Kinase Pathway in Yeast: Regulating Adaptation to Citric Acid Stress

2004 ◽  
Vol 24 (8) ◽  
pp. 3307-3323 ◽  
Author(s):  
Clare L. Lawrence ◽  
Catherine H. Botting ◽  
Robin Antrobus ◽  
Peter J. Coote
Keyword(s):  
Citric Acid ◽  
Protein Kinase ◽  
Mapk Pathway ◽  
Osmotic Shock ◽  
Acid Stress ◽  
Tca Cycle ◽  
Mitogen Activated Protein Kinase ◽  
High Osmolarity ◽  
High Osmolarity Glycerol ◽  
Mitogen Activated Protein

ABSTRACT Screening the Saccharomyces cerevisiae disruptome, profiling transcripts, and determining changes in protein expression have identified an important new role for the high-osmolarity glycerol (HOG) mitogen-activated protein kinase (MAPK) pathway in the regulation of adaptation to citric acid stress. Deletion of HOG1, SSK1, PBS2, PTC2, PTP2, and PTP3 resulted in sensitivity to citric acid. Furthermore, citric acid resulted in the dual phosphorylation, and thus activation, of Hog1p. Despite minor activation of glycerol biosynthesis, the inhibitory effect of citric acid was not due to an osmotic shock. HOG1 negatively regulated the expression of a number of proteins in response to citric acid stress, including Bmh1p. Evidence suggests that BMH1 is induced by citric acid to counteract the effect of amino acid starvation. In addition, deletion of BMH2 rendered cells sensitive to citric acid. Deletion of the transcription factor MSN4, which is known to be regulated by Bmh1p and Hog1p, had a similar effect. HOG1 was also required for citric acid-induced up-regulation of Ssa1p and Eno2p. To counteract the cation chelating activity of citric acid, the plasma membrane Ca2+ channel, CCH1, and a functional vacuolar membrane H+-ATPase were found to be essential for optimal adaptation. Also, the transcriptional regulator CYC8, which mediates glucose derepression, was required for adaptation to citric acid to allow cells to metabolize excess citrate via the tricarboxylic acid (TCA) cycle. Supporting this, Mdh1p and Idh1p, both TCA cycle enzymes, were up-regulated in response to citric acid.

scholarly journals Heat Stress Activates the Yeast High-Osmolarity Glycerol Mitogen-Activated Protein Kinase Pathway, and Protein Tyrosine Phosphatases Are Essential under Heat Stress

2002 ◽  
Vol 1 (2) ◽  
pp. 163-173 ◽  
Author(s):  
Astrid Winkler ◽  
Christopher Arkind ◽  
Christopher P. Mattison ◽  
Anne Burkholder ◽  
Kathryn Knoche ◽  
...  
Keyword(s):  
Heat Stress ◽  
Protein Kinase ◽  
Protein Tyrosine Phosphatases ◽  
Mitogen Activated Protein Kinase ◽  
Tyrosine Phosphatases ◽  
High Osmolarity ◽  
Protein Tyrosine ◽  
High Osmolarity Glycerol ◽  
Mitogen Activated Protein ◽  
Stress Activation

ABSTRACT The yeast high-osmolarity glycerol (HOG) mitogen-activated protein kinase (MAPK) pathway has been characterized as being activated solely by osmotic stress. In this work, we show that the Hog1 MAPK is also activated by heat stress and that Sho1, previously identified as a membrane-bound osmosensor, is required for heat stress activation of Hog1. The two-component signaling protein, Sln1, the second osmosensor in the HOG pathway, was not involved in heat stress activation of Hog1, suggesting that the Sho1 and Sln1 sensors discriminate between stresses. The possible function of Hog1 activation during heat stress was examined, and it was found that the hog1Δ strain does not recover as rapidly from heat stress as well as the wild type. It was also found that protein tyrosine phosphatases (PTPs) Ptp2 and Ptp3, which inactivate Hog1, have two functions during heat stress. First, they are essential for survival at elevated temperatures, preventing lethality due to Hog1 hyperactivation. Second, they block inappropriate cross talk between the HOG and the cell wall integrity MAPK pathways, suggesting that PTPs are important for maintaining specificity in MAPK signaling pathways.

scholarly journals Cdc37p Is Required for Stress-Induced High-Osmolarity Glycerol and Protein Kinase C Mitogen-Activated Protein Kinase Pathway Functionality by Interaction with Hog1p and Slt2p (Mpk1p)

2007 ◽  
Vol 6 (3) ◽  
pp. 521-532 ◽  
Author(s):  
Patricija Hawle ◽  
Danielle Horst ◽  
Jan Paul Bebelman ◽  
Xiao Xian Yang ◽  
Marco Siderius ◽  
...  
Keyword(s):  
Cell Wall ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Hog Pathway ◽  
High Osmolarity ◽  
High Osmolarity Glycerol ◽  
Kinase C ◽  
Mitogen Activated Protein

ABSTRACT The yeast Saccharomyces cerevisiae utilizes rapidly responding mitogen-activated protein kinase (MAPK) signaling cascades to adapt efficiently to a changing environment. Here we report that phosphorylation of Cdc37p, an Hsp90 cochaperone, by casein kinase 2 controls the functionality of two MAPK cascades in yeast. These pathways, the high-osmolarity glycerol (HOG) pathway and the cell integrity (protein kinase C) MAPK pathway, mediate adaptive responses to high osmotic and cell wall stresses, respectively. Mutation of the phosphorylation site Ser14 in Cdc37p renders cells sensitive to osmotic stress and cell wall perturbation by calcofluor white. We found that levels of the MAPKs Hog1p and Slt2p (Mpk1p) in cells are reduced in a cdc37-S14A mutant, and consequently downstream responses mediated by Hog1p and Slt2p are compromised. Furthermore, we present evidence that Hog1p and Slt2p both interact in a complex with Cdc37p in vivo, something that has not been reported previously. The interaction of Hsp90, Slt2p, and Hog1p with Cdc37p depends on the phosphorylation status of Cdc37p. In fact, our biochemical data show that the osmosensitive phenotype of the cdc37-S14A mutant is due to the loss of the interaction between Cdc37p, Hog1p, and Hsp90. Likewise, during cell wall stress, the interaction of Slt2p with Cdc37p and Hsp90 is crucial for Slt2p-dependent downstream responses, such as the activation of the transcription factor Rlm1p. Interestingly, phosphorylated Slt2p, but not phosphorylated Hog1p, has an increased affinity for Cdc37p. Together these observations suggest that Cdc37p acts as a regulator of MAPK signaling.

scholarly journals The High Osmolarity Glycerol Mitogen-Activated Protein Kinase regulates glucose catabolite repression in filamentous fungi

PLoS Genetics ◽  
2020 ◽  
Vol 16 (8) ◽  
pp. e1008996
Author(s):  
Leandro José de Assis ◽  
Lilian Pereira Silva ◽  
Li Liu ◽  
Kerstin Schmitt ◽  
Oliver Valerius ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Filamentous Fungi ◽  
Catabolite Repression ◽  
Mitogen Activated Protein Kinase ◽  
High Osmolarity ◽  
High Osmolarity Glycerol ◽  
Mitogen Activated Protein

Regulation of spontaneous and induced resumption of meiosis in mouse oocytes by different intracellular pathways

Reproduction ◽  
2000 ◽  
pp. 377-383 ◽  
Author(s):  
L Leonardsen ◽  
A Wiersma ◽  
M Baltsen ◽  
AG Byskov ◽  
CY Andersen
Keyword(s):  
Signal Transduction ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Mitogen Activated Protein Kinase ◽  
Meiotic Maturation ◽  
Mouse Oocytes ◽  
Mitogen Activated Protein ◽  
Dependent Signal ◽  
Kinase Pathway ◽  
Kinase A

The mitogen-activated protein kinase-dependent and the cAMP-protein kinase A-dependent signal transduction pathways were studied in cultured mouse oocytes during induced and spontaneous meiotic maturation. The role of the mitogen-activated protein kinase pathway was assessed using PD98059, which specifically inhibits mitogen-activated protein kinase 1 and 2 (that is, MEK1 and MEK2), which activates mitogen-activated protein kinase. The cAMP-dependent protein kinase was studied by treating oocytes with the protein kinase A inhibitor rp-cAMP. Inhibition of the mitogen-activated protein kinase pathway by PD98059 (25 micromol l(-1)) selectively inhibited the stimulatory effect on meiotic maturation by FSH and meiosis-activating sterol (that is, 4,4-dimethyl-5alpha-cholest-8,14, 24-triene-3beta-ol) in the presence of 4 mmol hypoxanthine l(-1), whereas spontaneous maturation in the absence of hypoxanthine was unaffected. This finding indicates that different signal transduction mechanisms are involved in induced and spontaneous maturation. The protein kinase A inhibitor rp-cAMP induced meiotic maturation in the presence of 4 mmol hypoxanthine l(-1), an effect that was additive to the maturation-promoting effect of FSH and meiosis-activating sterol, indicating that induced maturation also uses the cAMP-protein kinase A-dependent signal transduction pathway. In conclusion, induced and spontaneous maturation of mouse oocytes appear to use different signal transduction pathways.

Sign in / Sign up

Export Citation Format

Share Document