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ウシオダ リョウ
USHIODA RYO
潮田 亮 所属 京都産業大学 生命科学部 先端生命科学科 職種 准教授 |
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| 発行・発表の年月 | 2013/10/15 |
| 形態種別 | 研究論文 |
| 標題 | Glycosylation-independent ERAD pathway serves as a backup system under ER stress |
| 執筆形態 | その他 |
| 掲載誌名 | Molecular Biology of the Cell |
| 出版社・発行元 | American Society for Cell Biology (ASCB) |
| 巻・号・頁 | 24(20),3155-3163頁 |
| 著者・共著者 | Ryo Ushioda,Jun Hoseki,Kazuhiro Nagata |
| 概要 | During endoplasmic reticulum (ER)–associated degradation (ERAD), terminally misfolded proteins are retrotranslocated from the ER to the cytosol and degraded by the ubiquitin-proteasome system. Misfolded glycoproteins are recognized by calnexin and transferred to EDEM1, followed by the ER disulfide reductase ERdj5 and the BiP complex. The mechanisms involved in ERAD of nonglycoproteins, however, are poorly understood. Here we show that nonglycoprotein substrates are captured by BiP and then transferred to ERdj5 without going through the calnexin/EDEM1 pathway; after cleavage of disulfide bonds by ERdj5, the nonglycoproteins are transferred to the ERAD scaffold protein SEL1L by the aid of BiP for dislocation into the cytosol. When glucose trimming of the N-glycan groups of the substrates is inhibited, glycoproteins are also targeted to the nonglycoprotein ERAD pathway. These results indicate that two distinct pathways for ERAD of glycoproteins and nonglycoproteins exist in mammalian cells, and these pathways are interchangeable under ER stress conditions. |
| DOI | 10.1091/mbc.e13-03-0138 |
| ISSN | 1059-1524/1939-4586 |