Elucidation of the molecular mechanims of Parkin-PINK1 triggered mitophagy by using budding yeast
| Project/Area Number |
24657072
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Structural biochemistry
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| Research Institution | Nagoya University |
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Principal Investigator |
ENDO Toshiya 名古屋大学, 理学(系)研究科(研究院), 教授 (70152014)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 酵母 / ミトコンドリア / パーキンソン病 / PINK1 / Parkin |
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| Research Abstract |
In eukaryotic cells, aberrant mitochondria are selectively removed by a process called mitophagy, and PINK1 and Parkin, causative gene products for Parkinsonism, mediate this process in mammalian cells while yeast cells lack the Parkin-PINK1 system. Here we expressed Parkin and a PINK1 fusion protein that is artificially targeted to the mitochondrial outer membrane in yeast cells. Parkin expressed in the cytosol was recruited to the mitochondrial outer membrane by PINK1 in a manner that depends on the kinase activity of PINK1. The recruited Parkin was further phosphorylated and ubiquitinated like the case for mammalian cells. The yeast cells with artificially expressed Pakin-PINK1 can thus offer a useful tool to analyze the functions of the Parkin-PINK1 system.
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Report
(3 results)
Research Products
(20 results)
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[Journal Article] Ubiquitin is phosphorylated by PINK1 to activate parkin.2014
Author(s)
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., Endo, T., Fon. E. A., Trempe, J. F., Saeki, Y., Tanaka, K., and Matsuda, N.
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Journal Title
Nature
Volume: 510(in press)
Issue: 7503
Pages: 162-166
DOI
Related Report
Peer Reviewed
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