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エンドウ トシヤ
ENDO TOSHIYA
遠藤 斗志也 所属 京都産業大学 生命科学部 先端生命科学科 職種 客員教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2016/07 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Phosphatidylserine transport by Ups2-Mdm35 in respiration-active mitochondria |
| 執筆形態 | その他 |
| 掲載誌名 | JOURNAL OF CELL BIOLOGY |
| 出版社・発行元 | ROCKEFELLER UNIV PRESS |
| 巻・号・頁 | 214(1),pp.77-88 |
| 著者・共著者 | Non Miyata,Yasunori Watanabe,Yasushi Tamura,Toshiya Endo,Osamu Kuge |
| 概要 | Phosphatidylethanolamine (PE) is an essential phospholipid for mitochondrial functions and is synthesized mainly by phosphatidylserine (PS) decarboxylase at the mitochondrial inner membrane. In Saccharomyces cerevisiae, PS is synthesized in the endoplasmic reticulum (ER), such that mitochondrial PE synthesis requires PS transport from the ER to the mitochondria! inner membrane. Here, we provide evidence that Ups2-Mdm35, a protein complex localized at the mitochondrial intermembrane space, mediates PS transport for PE synthesis in respiration-active mitochondria. UPS2- and MDM35-null mutations greatly attenuated conversion of PS to PE in yeast cells growing logarithmically under nonfermentable conditions, but not fermentable conditions. A recombinant Ups2-Mdm35 fusion protein exhibited phospholipid-transfer activity between liposomes in vitro. Furthermore, UPS2 expression was elevated under nonfermentable conditions and at the diauxic shift, the metabolic transition from glycolysis to oxidative phosphorylation. These results demonstrate that Ups2-Mdm35 functions as a PS transfer protein and enhances mitochondrial PE synthesis in response to the cellular metabolic state. |
| DOI | 10.1083/jcb.201601082 |
| ISSN | 0021-9525/1540-8140 |
| PMID | 27354379 |