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Title: Yeast Hog1 proteins are sequestered in stress granules during high-temperature stress
Authors: Shiraishi, Kosuke  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-8780-9053 (unconfirmed)
Hioki, Takahiro
Habata, Akari
Yurimoto, Hiroya  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0001-7506-6184 (unconfirmed)
Sakai, Yasuyoshi  kyouindb  KAKEN_id
Author's alias: 白石, 晃將
日置, 貴大
幅田, 亜香莉
由里本, 博也
阪井, 康能
Keywords: High-temperature stress
Hog1
Stress granule
Yeast
Issue Date: Jan-2018
Publisher: Company of Biologists Ltd
Journal title: Journal of Cell Science
Volume: 131
Issue: 1
Thesis number: jcs.209114
Abstract: The yeast high-osmolarity glycerol (HOG) pathway plays a central role in stress responses. It is activated by various stresses, including hyperosmotic stress, oxidative stress, high-temperature stress and exposure to arsenite. Hog1, the crucial MAP kinase of the pathway, localizes to the nucleus in response to high osmotic concentrations, i.e. high osmolarity; but, otherwise, little is known about its intracellular dynamics and regulation. By using the methylotrophic yeast Candida boidinii, we found that CbHog1-Venus formed intracellular dot structures after high-temperature stress in a reversible manner. Microscopic observation revealed that CbHog1-mCherry colocalized with CbPab1-Venus, a marker protein of stress granules. Hog1 homologs in Pichia pastoris and Schizosaccharomyces pombe also exhibited similar dot formation under high-temperature stress, whereas Saccharomyces cerevisiae Hog1 (ScHog1)-GFP did not. Analysis of CbHog1-Venus in C. boidinii revealed that a β-sheet structure in the N-terminal region was necessary and sufficient for its localization to stress granules. Physiological studies revealed that sequestration of activated Hog1 proteins in stress granules was responsible for downregulation of Hog1 activity under high-temperature stress.
Rights: © 2018. Published by The Company of Biologists Ltd
URI: http://hdl.handle.net/2433/266866
DOI(Published Version): 10.1242/jcs.209114
PubMed ID: 29183915
Appears in Collections:Journal Articles

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