Complementary function of mitogen-activated protein kinase Hog1 from Trichosporonoides megachiliensis in Saccharomyces cerevisiae under hyper-osmotic stress

2013 ◽  
Vol 115 (2) ◽  
pp. 127-132 ◽  
Author(s):  
Junjiro Yoshida ◽  
Yosuke Kobayashi ◽  
Yosuke Tanaka ◽  
Yoshiyuki Koyama ◽  
Jun Ogihara ◽  
...  
Nutrients ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2440
Author(s):  
Lavinia Liliana Ruta ◽  
Ileana Cornelia Farcasanu

Caffeine–a methylxanthine analogue of the purine bases adenine and guanine–is by far the most consumed neuro-stimulant, being the active principle of widely consumed beverages such as coffee, tea, hot chocolate, and cola. While the best-known action of caffeine is to prevent sleepiness by blocking the adenosine receptors, caffeine exerts a pleiotropic effect on cells, which lead to the activation or inhibition of various cell integrity pathways. The aim of this review is to present the main studies set to investigate the effects of caffeine on cells using the model eukaryotic microorganism Saccharomyces cerevisiae, highlighting the caffeine synergy with external cell stressors, such as irradiation or exposure to various chemical hazards, including cigarette smoke or chemical carcinogens. The review also focuses on the importance of caffeine-related yeast phenotypes used to resolve molecular mechanisms involved in cell signaling through conserved pathways, such as target of rapamycin (TOR) signaling, Pkc1-Mpk1 mitogen activated protein kinase (MAPK) cascade, or Ras/cAMP protein kinase A (PKA) pathway.


2019 ◽  
Vol 12 (609) ◽  
pp. eaaw4956
Author(s):  
Angel Guerra-Moreno ◽  
Miguel A. Prado ◽  
Jessie Ang ◽  
Helena M. Schnell ◽  
Yagmur Micoogullari ◽  
...  

The yeast stress-activated protein kinase Hog1 is best known for its role in mediating the response to osmotic stress, but it is also activated by various mechanistically distinct environmental stressors, including heat shock, endoplasmic reticulum stress, and arsenic. In the osmotic stress response, the signal is sensed upstream and relayed to Hog1 through a kinase cascade. Here, we identified a mode of Hog1 function whereby Hog1 senses arsenic through a direct physical interaction that requires three conserved cysteine residues located adjacent to the catalytic loop. These residues were essential for Hog1-mediated protection against arsenic, were dispensable for the response to osmotic stress, and promoted the nuclear localization of Hog1 upon exposure of cells to arsenic. Hog1 promoted arsenic detoxification by stimulating phosphorylation of the transcription factor Yap8, promoting Yap8 nuclear localization, and stimulating the transcription of the only known Yap8 targets, ARR2 and ARR3, both of which encode proteins that promote arsenic efflux. The related human kinases ERK1 and ERK2 also bound to arsenic in vitro, suggesting that this may be a conserved feature of some members of the mitogen-activated protein kinase (MAPK) family. These data provide a mechanistic basis for understanding how stress-activated kinases can sense distinct threats and perform highly specific adaptive responses.


2013 ◽  
Vol 24 (19) ◽  
pp. 3145-3154 ◽  
Author(s):  
Xia Li ◽  
Susan Ferro-Novick ◽  
Peter Novick

Ptc1p, a type 2C protein phosphatase, is required for a late step in cortical endoplasmic reticulum (cER) inheritance in Saccharomyces cerevisiae. In ptc1Δ cells, ER tubules migrate from the mother cell and contact the bud tip, yet fail to spread around the bud cortex. This defect results from the failure to inactivate a bud tip–associated pool of the cell wall integrity mitogen-activated protein kinase, Slt2p. Here we report that the polarisome complex affects cER inheritance through its effects on Slt2p, with different components playing distinct roles: Spa2p and Pea2p are required for Slt2p retention at the bud tip, whereas Bni1p, Bud6p, and Sph1p affect the level of Slt2p activation. Depolymerization of actin relieves the ptc1Δ cER inheritance defect, suggesting that in this mutant the ER becomes trapped on the cytoskeleton. Loss of Sec3p also blocks ER inheritance, and, as in ptc1Δ cells, this block is accompanied by activation of Slt2p and is reversed by depolymerization of actin. Our results point to a common mechanism for the regulation of ER inheritance in which Slt2p activity at the bud tip controls the association of the ER with the actin-based cytoskeleton.


2005 ◽  
Vol 4 (11) ◽  
pp. 1785-1793 ◽  
Author(s):  
Isabelle Dunand-Sauthier ◽  
Carol A. Walker ◽  
Jana Narasimhan ◽  
Amanda K. Pearce ◽  
Ronald C. Wek ◽  
...  

ABSTRACT The stress-activated protein kinase (SAPK) pathway plays a central role in coordinating gene expression in response to diverse environmental stress stimuli. We examined the role of this pathway in the translational response to stress in Schizosaccharomyces pombe. Exposing wild-type cells to osmotic stress (KCl) resulted in a rapid but transient reduction in protein synthesis. Protein synthesis was further reduced in mutants disrupting the SAPK pathway, including the mitogen-activated protein kinase Wis1 or the mitogen-activated protein kinase Spc1/Sty1, suggesting a role for these stress response factors in this translational control. Further polysome analyses revealed a role for Spc1 in supporting translation initiation during osmotic stress, and additionally in facilitating translational adaptation. Exposure to oxidative stress (H2O2) resulted in a striking reduction in translation initiation in wild-type cells, which was further reduced in spc1 − cells. Reduced translation initiation correlated with phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF2α) in wild-type cells. Disruption of Wis1 or Spc1 kinase or the downstream bZip transcription factors Atf1 and Pap1 resulted in a marked increase in eIF2α phosphorylation which was dependent on the eIF2α kinases Hri2 and Gcn2. These findings suggest a role for the SAPK pathway in supporting translation initiation and facilitating adaptation to environmental stress in part through reducing eIF2α phosphorylation in fission yeast.


2012 ◽  
Vol 25 (6) ◽  
pp. 802-816 ◽  
Author(s):  
Jens Heller ◽  
Nadja Ruhnke ◽  
José Juan Espino ◽  
Michelli Massaroli ◽  
Isidro Gonzalez Collado ◽  
...  

The mitogen-activated protein kinase (MAPK) BcSak1 of Botrytis cinerea is activated upon exposure to H2O2 and, hence, might be involved in coping with oxidative stress during infection. However, beside osmotic and oxidative stress sensitivity, Δbcsak1 mutants have a pleiotropic phenotype, as they do not produce conidia and are unable to penetrate unwounded host tissue. In this study, the role of BcSak1 was investigated in the stress response and during infection of French beans by Botrytis cinerea. Using a macroarray approach, it was shown that BcSak1 is only marginally involved in the specific oxidative stress response. In fact, the induction of several genes after oxidative stress treatment is BcSak1-dependent, but most of these genes are also induced under conditions of osmotic stress. The majority of genes regulated by BcSak1 are not involved in the stress response at all. Using a translational fusion of BcSak1 to green fluorescent protein, it was shown clearly that the localization of this MAPK depends on the type of stress being applied; it associates rapidly to the nucleus only under osmotic stress. Therefore, a model is proposed in which BcSak1 acts in the cytosol by activation of one or more transcription factors under oxidative stress and, at the same time, it reacts to osmotic stress by migrating to the nucleus. Interestingly, the MAPK is also involved in the regulation of secondary metabolism, as the major phytotoxins secreted by this fungus are reduced in the Δbcsak1 deletion mutant. Experiments done in planta underlined the essential role of BcSak1 in the early stages of infection, when it translocates to the nucleus and then changes to cytosolic distribution during hyphal growth within the tissue.


1997 ◽  
Vol 17 (5) ◽  
pp. 2615-2623 ◽  
Author(s):  
Y Watanabe ◽  
G Takaesu ◽  
M Hagiwara ◽  
K Irie ◽  
K Matsumoto

The Mpk1 (Slt2) mitogen-activated protein (MAP) kinase has been implicated in several biological processes in Saccharomyces cerevisiae. The Rlm1 protein, a member of the MADS box family of transcription factors, functions downstream of Mpk1 in the pathway. To characterize the role of Rlm1 in mediating the transcriptional activation by the Mpk1 pathway, we constructed a LexA-Rlm1 deltaN chimera in which sequences, including the MADS box domain of the Rlm1 protein, were replaced by the LexA DNA binding domain and tested the ability of this chimera to activate a LexA operator-controlled reporter gene. In this assay, the Rlm1 protein was found to activate transcription in a manner regulated by the Mpk1 pathway. The Mpk1 protein kinase phosphorylated Rlm1 deltaN in vitro and the LexA-Rlm1 deltaN chimera protein was phosphorylated in vivo in a Mpk1-dependent manner. These results suggest that Mpk1 regulates the transcriptional activity of Rlm1 by directly phosphorylating it. We identified a Mpk1-like protein kinase, Mlp1, as an Rlm1-associated protein by using the yeast two-hybrid system. Overexpression of MLP1 suppresses the caffeine-sensitive phenotype of the bck1 delta mutation. The additivity of the mlp1 delta defect with the Mpk1 delta defect with regard to the caffeine sensitivity, combined with the results of genetic epistasis experiments, suggested that the activity of Rlm1 is regulated independently by Mpk1 MAP kinase and the Mlp1 MAP kinase-like kinase.


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