| 研究課題/領域番号 |
23KF0055
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| 研究種目 |
特別研究員奨励費
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| 配分区分 | 基金 |
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| 応募区分 | 外国 |
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| 審査区分 |
小区分44030:植物分子および生理科学関連
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| 研究機関 | 広島大学 |
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研究代表者 |
坂本 敦 広島大学, 統合生命科学研究科(理), 教授 (60270477)
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| 研究分担者 |
ABEDI TAYEBEH 広島大学, 統合生命科学研究科(理), 外国人特別研究員
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| 研究期間 (年度) |
2023-04-25 – 2024-03-31
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| 研究課題ステータス |
中途終了 (2023年度)
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| 配分額 *注記 |
2,000千円 (直接経費: 2,000千円)
2024年度: 1,000千円 (直接経費: 1,000千円)
2023年度: 1,000千円 (直接経費: 1,000千円)
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| キーワード | Phytohormone / Organellar dynamics / Endoplasmic reticulum |
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| 研究開始時の研究の概要 |
Abscisic acid (ABA) regulates plant responses and adaption to stress. Although accumulated ABA triggers such plant-physiological processes, how plants rapidly produce ABA remains to be elucidated. ABA is produced by the multi-step biosynthesis and the single-step hydrolysis of inactive ABA glucosides. Recently, we reported that the latter reaction occurs quickly preceding the former and is activated by stress-induced organellar dynamics involving membrane protein trafficking. We will investigate the mechanism for such quick ABA production as a crucial early step for plant stress adaptation.
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| 研究実績の概要 |
Abscisic acid (ABA) regulates plant responses and adaption to stress, allowing plants to survive in hostile environments. Although cellular ABA accumulation triggers a series of such plant-physiological processes, how plants rapidly produce ABA upon the onset of stress remains to be elucidated. ABA is produced by the multi-step biosynthesis and the single-step hydrolysis of inactive ABA-glucoside conjugates. We recently reported that the latter reaction occurs quickly preceding the former and is likely activated by stress-induced endoplasmic reticulum dynamics involving protein trafficking. To elucidate quick ABA production as a crucial early step for plant stress adaptation, this study examined the behavior of a major enzyme responsible for ABA-glucoside hydrolysis in response to stress conditions by using confocal laser scanning microscopy, immunoblotting, and immuno-electron microscopy. Even though the research project had to be terminated less than ten months after its inception due to unavoidable circumstances with a fellow researcher, the obtained results suggested that such organellar dynamics cause alteration in the enzyme's subcellular localization, which would facilitate quick access of the enzyme to its substrate stored in different compartments.
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