| Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Outline of Final Research Achievements |
Eukaryotic cells cumulatively evoke the endoplasmic reticulum (ER)-stress response or the unfolded protein response (UPR). Cellular stress causing the UPR has been believed to accompany accumulation of unfolded proteins in the ER. In consistent to this idea, ER stress sensors including the ER-located type-I transmembrane protein Ire1 is activated through ER accumulation of unfolded proteins. However, recent studies revealed that membrane-lipid abnormalities and/or disturbance of intracellular respiration also cause ER stress which initiates the UPR. In the present study, I have addressed modulation of Ire1’s activity by mitochondrial dysfunction in yeast Saccharomyces cerevisiae cells. Namely, Ire1 gets insensitive to weak ER stress in cells lacking normal mitochondrial function.
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