Physiological roles of ER-associated degradation beyond the protein quality control
| Project/Area Number |
15K18503
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 小胞体 / 品質管理 / ユビキチン / 金属イオン輸送体 / ERAD / 品質管理機構 / タンパク質分解 / タンパク質 / プロテアソーム |
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| Outline of Final Research Achievements |
In the course of this study, I focused on the analysis of Cdc99, which is a cell-cycle related protein. In the ERAD defective strain, the expression of endogenous Cdc99 increased. However, because Cdc99 degradation was not significantly affected by the depletion of ERAD-related components, the transcription of Cdc99 might have been upregulated in ERAD defective strains. I am currently testing this hypothesis.
In this study, I also found a novel genetic interaction between ERAD and metal ion transport. I am currently testing if this interaction is mediated by Cdc99.
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Report
(3 results)
Research Products
(16 results)
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[Journal Article] The ubiquitin ligase SCFUcc1 acts as a metabolic switch for the glyoxylate cycle.2015
Author(s)
Nakatsukasa, K., Nishimura, T., Byrne, D., Okamoto, M., Takahashi-Nakaguchi, A., Chibana, H., Okumura, F., Kamura, T.
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Journal Title
Molecular Cell
Volume: 59
Issue: 1
Pages: 22-34
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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