| 研究課題/領域番号 |
21K20632
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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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| キーワード | Mitophagy / Atg32 / Ppg1 / The Far complex / Yeast / Autophagy |
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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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| 次年度使用額が生じた理由 |
Because of the delay caused by problems with Far8 substitution mutants plasmids, I had to move experiments with Atg32-Far complex purification to the next fiscal year.
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