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Dissection of the HOG pathway activated by hydrogen peroxide in Saccharomyces cerevisiae

Title
Dissection of the HOG pathway activated by hydrogen peroxide in Saccharomyces cerevisiae
Authors
Lee, Young MiKim, EunjungAn, JieunLee, YejiChoi, EunyongChoi, WonjaMoon, EunpyoKim, Wankee
Ewha Authors
최원자
SCOPUS Author ID
최원자scopus
Issue Date
2017
Journal Title
ENVIRONMENTAL MICROBIOLOGY
ISSN
1462-2912JCR Link1462-2920JCR Link
Citation
vol. 19, no. 2, pp. 584 - 597
Publisher
WILEY
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Cells usually cope with oxidative stress by activating signal transduction pathways. In the budding yeast Sacchromyces cerevisiae, the high osmolarity glycerol (HOG) pathway has long been implicated in transducing the oxidative stress-induced signal, but the underlying mechanisms are not well defined. Based on phosphorylation of the mitogen-activated protein kinase (MAPK) Hog1, we reveal that the signal from hydrogen peroxide (H2O2) flows through Ssk1, the response regulator of the two-component system of the HOG pathway. Downstream signal transduction into the HOG MAPK cascade requires the MAP kinase kinase kinase (MAP3K) Ssk2 but not its paralog Ssk22 or another MAP3K Ste11 of the pathway, culminating in Hog1 phosphorylation via the MAP2K Pbs2. When overexpressed, Ssk2 is also activated in an Ssk1-independent manner. Unlike in mammals, H2O2 does not cause endoplasmic reticulum stress, which can activate Hog1 through the conventional unfolded protein response. Hog1 activated by H2O2 is retained in the cytoplasm, but is still able to activate the cAMP- or stress-responsive elements by unknown mechanisms.
DOI
10.1111/1462-2920.13499
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
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