| 研究課題/領域番号 |
21K20632
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| 研究種目 |
研究活動スタート支援
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| 配分区分 | 基金 |
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| 審査区分 |
0701:分子レベルから細胞レベルの生物学およびその関連分野
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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) |
2021-08-30 – 2023-03-31
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| 研究課題ステータス |
交付 (2021年度)
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| 配分額 *注記 |
3,120千円 (直接経費: 2,400千円、間接経費: 720千円)
2022年度: 1,560千円 (直接経費: 1,200千円、間接経費: 360千円)
2021年度: 1,560千円 (直接経費: 1,200千円、間接経費: 360千円)
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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 mitophagy receptor Atg32 is essential for mitophagy and antagonistically regulated by CK2 and Ppg1. The Ppg1-binding partner Far complex interacts with Atg32 and this interaction is impaired upon mitophagy stimuli, leading to Atg32 phosphorylation, but the underlying mechanism still unclear. To investigate the Far complex-mediated mitophagy regulation in yeast, this study aims to elucidate: ① How the Far complex and Atg32 interact; ② the upstream signalling pathway regulating this interaction.
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| 研究実績の概要 |
Mitophagy contributes to maintaining mitochondrial quality and quantity. The phosphorylation of Atg32 is essential for mitophagy. The Far complex interacts with Atg32 to phosphorylate it, but the underlying mechanism is still unclear. Therefore, this study aims to elucidate: 1) How the Far complex and Atg32 interact 2) the upstream signalling pathway regulating this interaction. So far I elucidated the next points: 1) None of genomically substituted Far8 phosphorylation sites mutants affected Atg32 phosphorylation status and Far8-Atg32 interaction. 2) I Found out that Far3/7-Atg32 interaction is mediated by Far8. Far3 and Far7 (parts of the Far complex) are necessary for Far8-Atg32 interaction.
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| 現在までの達成度 (区分) |
現在までの達成度 (区分)
3: やや遅れている
理由
I had some problems with protein expression of plasmids for Far8 substitution mutants and I had to change strategy to genomic integration of Far8 substitution mutations, which takes longer time compared to construction of plasmids with substitution mutations
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| 今後の研究の推進方策 |
Next, I am planing to purify Atg32-Far complex for further Cryo-electron microspoic analysis of the bound state structure of Atg32-Far complex. Then, I am also planning to find out alternative posttranslational modification of Far8 and upstream singnaling pathway which regulate association and dissociation of Far8-Atg32 interaction.
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