| Project/Area Number |
24370081
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
KIMATA Yukio 奈良先端科学技術大学院大学, バイオサイエンス研究科, 准教授 (60263448)
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| Co-Investigator(Kenkyū-buntansha) |
斉藤 美知子 (斉藤 美智子) 奈良先端科学技術大学院大学, バイオサイエンス研究科, 助教 (40379558)
柳谷 耕太 奈良先端科学技術大学院大学, バイオサイエンス研究科, 特任助教 (70614775)
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| Co-Investigator(Renkei-kenkyūsha) |
KOHNO Kenji 奈良先端科学技術大学院大学, バイオサイエンス研究科, 教授 (50142005)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥18,200,000 (Direct Cost: ¥14,000,000、Indirect Cost: ¥4,200,000)
Fiscal Year 2014: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥6,110,000 (Direct Cost: ¥4,700,000、Indirect Cost: ¥1,410,000)
Fiscal Year 2012: ¥6,760,000 (Direct Cost: ¥5,200,000、Indirect Cost: ¥1,560,000)
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| Keywords | 小胞体 / オルガネラ / 酵母 / ストレス応答 / ストレス / 膜脂質 / 微生物 / 出芽酵母 |
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| Outline of Final Research Achievements |
The endoplasmic reticulum (ER) is a cellular compartment in which secretory proteins are folded and membrane lipids are metabolized. ER stress, namely dysfunction of the ER, has been believed to be caused by impaired protein folding in the ER, which leads to formation of toxic aggregates of denatured proteins. ER stress activates the ER-located transmembrane protein Ire1, which evokes the unfolded protein response (UPR) to protect cells against ER stress. In the present study, we addressed how membrane-lipid aberrancy activates Ire1 and evokes the UPR. In budding yeast cells, mutant Ire1 which cannot recognize unfolded proteins was normally activated by disturbance of membrane-lipid homeostasis. Also through analysis of proteins which are associated with Ire1 in yeast cells, we could establish a molecular model which explains activation of Ire1 by membrane-lipid aberrancy.
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