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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 | 2010/03 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | A vacuolar carboxypeptidase mutant of Arabidopsis thaliana is degraded by the ERAD pathway independently of its N-glycan |
| 執筆形態 | その他 |
| 掲載誌名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS |
| 出版社・発行元 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| 巻・号・頁 | 393(3),pp.384-389 |
| 著者・共著者 | Masaya Yamamoto,Mitsuyoshi Kawanabe,Yoko Hayashi,Toshiya Endo,Shuh-ichi Nishikawa |
| 概要 | Misfolded proteins produced in the endoplasmic reticulum (ER) are degraded by a mechanism, the ER-associated degradation (ERAD). Here we report establishment of the experimental system to analyze the ERAD in plant cells. Carboxypeptidase V (CPY) is a vacuolar enzyme and its mutant CPY* is degraded by the ERAD in yeast. Since Arabidopsis thaliana has AtCPY, an ortholog of yeast CPY, we constructed and expressed fusion proteins consisting of AtCPY and GFP and of AtCPY*, which carries a mutation homologous to yeast CPY* and GFP in A. thaliana cells. While AtCPY-GFP was efficiently transported to the vacuole, AtCPY* -GFP was retained in the ER to be degraded in proteasome- and Cdc48-dependent manners. We also found that AtCPY*-GFP was degraded by the ERAD in yeast cells, but that its single N-glycan did not function as a degradation signal in yeast or plant cells. Therefore, AtCPY*-GFP can be used as a marker protein to analyze the ERAD pathway, likely for nonglycosylated substrates, in plant cells. (C) 2010 Elsevier Inc. All rights reserved. |
| DOI | 10.1016/j.bbrc.2010.02.001 |
| ISSN | 0006-291X |