| 研究課題/領域番号 |
22K15058
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| 研究種目 |
若手研究
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| 配分区分 | 基金 |
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| 審査区分 |
小区分43030:機能生物化学関連
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| 研究機関 | 新潟大学 |
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研究代表者 |
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| 研究期間 (年度) |
2022-04-01 – 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 |
4,680千円 (直接経費: 3,600千円、間接経費: 1,080千円)
2023年度: 2,340千円 (直接経費: 1,800千円、間接経費: 540千円)
2022年度: 2,340千円 (直接経費: 1,800千円、間接経費: 540千円)
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| キーワード | Mitophagy / Atg32 / Ppg1 / The Far complex / Yeast / Autophagy |
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| 研究開始時の研究の概要 |
Mitophagy contributes to maintaining mitochondrial quality and quantity. The phosphorylation of the Atg32 is essential for mitophagy and is antagonistically regulated by CK2 and Ppg1. The Ppg1-binding partner Far complex is involved in Atg32 dephosphorylation. Apart from Atg32-Far8, interaction important for mitophagy regulation, it was found that Far3/Far7 interact with Atg32 independently of Far8. Thus, this study aims to clarify
① the structural basis for interaction between Far3/Far7 and Atg32
② the upstream signaling pathway regulating the dissociation between the Far complex and Atg32
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| 研究実績の概要 |
Mitophagy sustains mitochondrial quality and quantity via Atg32 phosphorylation, involving the enigmatic Far complex interaction. This study seeked to clarify: 1) Far3/7's interplay with Atg32 2) The upstream signaling guiding this interaction.
Interestingly, experiments with Far3/7 phosphorylation mutants revealed no disruption in the Atg32-Far complex interaction. Exploring Far3/7 expression and degradation effects yielded no discernible impact. Likewise, autophagy-associated kinase assessment failed to influence the Atg32-Far complex connection. These findings underscore the intricate regulatory mechanisms behind mitophagy. While specifics of Atg32-Far complex interaction remain elusive, this study contributes to our understanding of mitochondrial quality and quantity control.
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