2022 Fiscal Year Annual Research Report
Structural and molecular basis of the mitophagy regulation mediated by the Far complex in yeast
| Project/Area Number |
21K20632
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| Research Institution | Niigata University |
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Principal Investigator |
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| Project Period (FY) |
2021-08-30 – 2023-03-31
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| Keywords | Mitophagy / Atg32 / Ppg1 / The Far complex / Yeast / Autophagy |
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| Outline of Annual Research Achievements |
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. After finding out that substitution mutants of Far8 phosphorylation sites do not influence the Atg32-Far8 interaction, I have checked if it is regulated by expression level or degradation of Far8 or not. Neither expression or degradation of Far8 seemed to influence the interaction. Additionally, I checked influence of set of kinases involved in autophagy, but non of them had influence on Atg32-Far8 interaction.
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