2013 Fiscal Year Final Research Report
The mechanism of Drp1-dependent mitochondrial fission
| Project/Area Number |
24657138
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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 |
Cell biology
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| Research Institution | Kyushu University |
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Principal Investigator |
MIHARA Katsuyoshi 九州大学, 医学(系)研究科(研究院), 名誉教授 (40029963)
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| Co-Investigator(Kenkyū-buntansha) |
岡 敏彦 九州大学, 医学研究院, 准教授 (40263321)
大寺 秀典 九州大学, 医学研究院, 助教 (40380612)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | ミトコンドリア / ミトコンドリア分裂 / ミトコンドリア融合 / Drp1 / Mff / Mid49 / Mid51 |
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| Research Abstract |
Mitochondria participate in a variety of physiologic processes such as the ATP poroduction and apoptosis. Mitochondria dynamically change morphology through fusion and fission and high MW GTPases Mfn1 and Mfn2 of outer membrane and OPA1 of inner membrane are involved in fusion, whereas cytoplasimic Drp1 regulates fission. Here, (1) Since outer membrane proteins Mff, Mid49 and Mid51 function as the Drp1 receptor, we analyzed relative importance of these receptors and found that Mff as the major Drp1 receptor. (2) We have generated Mff-KO mice; they were embryonic lethal (E6.5). Consideing that Drp1-KO mice are lethal at E12.5, Mff seems to have important developmental function in addition to the Drp1-receptor function. Furhtermore, we have demonstrated that (3) Drp1 is involved in segregation of mitochondrial nucleoids, Drp1 is esssential for making correctly arranged heart mucle fibers, and konckout of liver Drp1 induced NASH phenotype in high fat diet-fed rats by the ER stress.
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[Journal Article] Fis1 acts as mitochondrial recruitment factor for TBC1D15 that involved in regulation of mitochondrial morphology2013
Author(s)
K. Onoue, A. Jofuku, R. Ban-Ishihara, T. Ishihara, M. Maeda, T. Koshiba, T. Itoh, Fukuda, H. Otera, T. Oka, H. Takano, Mizushima, K. Mihara and N. Ishihara.
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Journal Title
JCS
Volume: 126 (pt 1)
Pages: 176-185
DOI
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[Journal Article] PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria2012
Author(s)
Okatsu, T. Oka, M. Iguchi, K. Imamura, H. Kosako, N. Tani, M. Kimura, E. Go, F. Koyano, M. Funayama, K. Shiba-Fukushima, S. Sato, H. Shimizu, Y. Fukunaga, H. Taniguchi, M. Kamatsu, N. Hattori, K. Mihara, K. Tanaka, and N. Matsuda.
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Journal Title
Nature Communications
Volume: 3,1016
Pages: 1-10
DOI
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