| アイテムタイプ |
文献 / Documents(1) |
| 公開日 |
2021-11-08 |
| アクセス権 |
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アクセス権 |
open access |
| 資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
| 出版社版DOI |
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関連識別子 |
https://doi.org/10.3390/biology10111112 |
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関連名称 |
10.3390/biology10111112 |
| 出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| タイトル |
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タイトル |
Functional Interplay between P5 and PDI/ERp72 to Drive Protein Folding |
| 著者 |
松﨑, 元紀
オカダ, リナ
タニカワ, ユウヤ
カネムラ, シンゴ
イトウ, ダイ
Lin, Yuxi
ワタベ, マイ
ヤマグチ, ヒロシ
齋尾, 智英
Lee, Young-Ho
イナバ, ケンジ
オクムラ, マサキ
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| 抄録 |
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内容記述 |
The physiological functions of proteins are destined by their unique three-dimensional structures. Almost all biological kingdoms share conserved disulfide-catalysts and chaperone networks that assist in correct protein folding and prevent aggregation. Disruption of these networks is implicated in pathogenesis, including neurodegenerative disease. In the mammalian endoplasmic reticulum (ER), more than 20 members of the protein disulfide isomerase family (PDIs) are believed to cooperate in the client folding pathway, but it remains unclear whether complex formation among PDIs via non-covalent interaction is involved in regulating their enzymatic and chaperone functions. Herein, we report novel functional hetero complexes between PDIs that promote oxidative folding and inhibit aggregation along client folding. The findings provide insight into the physiological significance of disulfide-catalyst and chaperone networks and clues for understanding pathogenesis associated with disruption of the networks. |
| 抄録 |
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内容記述 |
P5 is one of protein disulfide isomerase family proteins (PDIs) involved in endoplasmic reticulum (ER) protein quality control that assists oxidative folding, inhibits protein aggregation, and regulates the unfolded protein response. P5 reportedly interacts with other PDIs via intermolecular disulfide bonds in cultured cells, but it remains unclear whether complex formation between P5 and other PDIs is involved in regulating enzymatic and chaperone functions. Herein, we established the far-western blot method to detect non-covalent interactions between P5 and other PDIs and found that PDI and ERp72 are partner proteins of P5. The enzymatic activity of P5-mediated oxidative folding is up-regulated by PDI, while the chaperone activity of P5 is stimulated by ERp72. These findings shed light on the mechanism by which the complex formations among PDIs drive to synergistically accelerate protein folding and prevents aggregation. This knowledge has implications for understanding misfolding-related pathology. |
| キーワード |
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主題 |
protein disulfide isomerase family |
| キーワード |
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主題 |
disulfide bond |
| キーワード |
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|
主題 |
endoplasmic reticulum |
| キーワード |
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主題 |
oxidative folding |
| キーワード |
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主題 |
molecular chaperone |
| キーワード |
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主題 |
protein-protein interaction |
| 書誌情報 |
en : Biology
巻 10,
号 11,
p. 1112,
発行日 2021-10-28
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| 収録物ID |
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
20797737 |
| 出版者 |
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出版者 |
MDPI |
| 権利情報 |
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|
権利情報 |
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
| EID |
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識別子 |
382918 |
| 言語 |
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言語 |
eng |
biology_10_11_1112.pdf (2.13 MB)
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