2022 Fiscal Year Final 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 Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Multi-year Fund |
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| Review Section |
0701:Biology at molecular to cellular levels, and related fields
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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 |
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| Outline of Final Research Achievements |
Mitophagy is crucial for maintaining mitochondrial quality and quantity, with phosphorylation of Atg32 being an essential step. However, the underlying mechanism of the Far complex's interaction with Atg32 to phosphorylate it is still unclear. This study aimed to elucidate the interaction between the Far complex and Atg32, as well as the upstream signaling pathway regulating it. The study found that substitution mutants of Far8 phosphorylation sites do not affect Atg32 phosphorylation status or Far8-Atg32 interaction. Additionally, the study discovered that Far3 and Far7 are necessary for Far8-Atg32 interaction. The study also checked the influence of the expression level or degradation of Far8, as well as the influence of a set of kinases involved in autophagy, but neither seemed to affect the Atg32-Far8 interaction.
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| Free Research Field |
Cellular physiology
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| Academic Significance and Societal Importance of the Research Achievements |
This research could help researchers understand regulation of autophagy, mitophagy in particular. These findings could also lead to new insights into cellular signaling pathways and potentially aid in the development of new therapeutics for diseases caused by mitochondrial dysfunction.
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