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An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response
http://hdl.handle.net/10061/0002000511
http://hdl.handle.net/10061/0002000511ff4a1b32-81ee-4c82-861f-db67c1d7dc8e
| 名前 / ファイル | ライセンス | アクション |
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fulltext (377 KB)
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| アイテムタイプ | 学術雑誌論文 / Journal Article(1) | |||||||
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| 公開日 | 2024-08-05 | |||||||
| タイトル | ||||||||
| タイトル | An ER-accumulated mutant of yeast Pma1 causes membrane-related stress to induce the unfolded protein response | |||||||
| 言語 | ||||||||
| 言語 | eng | |||||||
| キーワード | ||||||||
| 主題Scheme | Other | |||||||
| 主題 | Unfolded protein response | |||||||
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| 主題Scheme | Other | |||||||
| 主題 | Endoplasmic reticulum | |||||||
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| 主題Scheme | Other | |||||||
| 主題 | Yeast | |||||||
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| 主題Scheme | Other | |||||||
| 主題 | Lipid bilayer stress | |||||||
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| 主題Scheme | UDC | |||||||
| 主題 | Saccharomyces cerevisiae | |||||||
| 資源タイプ | ||||||||
| 資源タイプ | journal article | |||||||
| アクセス権 | ||||||||
| アクセス権 | open access | |||||||
| 著者 |
Phuong, Huong Thi
× Phuong, Huong Thi
× 木俣, 有紀× 木俣, 行雄 |
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| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | Upon dysfunction of the endoplasmic reticulum (ER), namely ER stress, eukaryotic cells provoke the unfolded protein response (UPR), which is triggered by ER stress sensors including Ire1. While the ER luminal domain of Ire1 is known to directly recognize misfolded soluble proteins accumulated in the ER, the transmembrane domain of Ire1 is involved in its self-association and activation upon membrane lipid-related abnormalities, which are so-called lipid bilayer stress (LBS). Here we inquired how the ER accumulation of misfolded transmembrane proteins induces the UPR. In yeast Saccharomyces cerevisiae cells, a multi-transmembrane protein, Pma1, is not transported to the cell surface but aggregates on the ER membrane when carrying a point mutation (Pma1-2308). Here, we show that GFP-tagged Ire1 co-localized with the Pma1-2308-mCherry puncta. This co-localization and the UPR induced by Pma1-2308-mCherry were compromised by a point mutation in Ire1 that specifically impairs its activation upon LBS. We presume that Pma1-2308-mCherry locally affects the properties (probably the thickness) of the ER membrane at its aggregation sites, where Ire1 is then recruited, self-associated, and then activated. | |||||||
| 書誌情報 |
en : Biochemical and Biophysical Research Communications 巻 667, p. 58-63, 発行日 2023-05-13 |
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| 出版者 | Elsevier | |||||||
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| 収録物識別子タイプ | EISSN | |||||||
| 収録物識別子 | 0006-291X | |||||||
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| 関連タイプ | isVersionOf | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | https://doi.org/10.1016/j.bbrc.2023.05.044 | |||||||
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| 関連タイプ | isVersionOf | |||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | https://www.sciencedirect.com/science/article/pii/S0006291X23006071 | |||||||
| 権利 | ||||||||
| 権利情報 | $00A9 2023 Elsevier Inc. All rights reserved. $00A9 2023. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/ | |||||||
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| 出版タイプ | AM | |||||||
