|
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 |
|
| 言語種別 | 英語 |
| 発行・発表の年月 | 2001/05 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation |
| 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 | 153(5),pp.1061-1069 |
| 著者・共著者 | S Nishikawa,SW Fewell,Y Kato,JL Brodsky,T Endo |
| 概要 | Endoplasmic reticulum (ER)-associated degradation (ERAD) is the process by which aberrant proteins in the ER lumen are exported back to the cytosol and degraded by the proteasome. Although ER molecular chaperones are required for ERAD, their specific role(s) in this process have been ill defined. To understand how one group of interacting lumenal chaperones facilitates ERAD, the fates of pro-cr-factor and a mutant form of carboxypeptidase Y were examined both in vivo and in vitro. We found that these ERAD substrates are stabilized and aggregate in the ER at elevated temperatures when BiP, the Lumenal Hsp70 molecular chaperone, is mutated, or when the genes encoding the J domain-containing proteins Jem1p and SCJ1 are deleted. In contrast, deletion of JEM1 and SCJ1 had little effect on the ERAD of a membrane protein. These results suggest that one role of the BiP, Jem1p, and Scj1p chaperones is to maintain lumenal ERAD substrates in a retrotranslocation-competent state. |
| ISSN | 0021-9525/1540-8140 |