| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2021-11-25 |
| タイトル |
|
|
タイトル |
Stepwise Assembly of Fibrinogen Is Assisted by the Endoplasmic Reticulum Lectin-Chaperone System in HepG2 Cells |
|
言語 |
en |
| 言語 |
|
|
言語 |
eng |
| 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 |
| アクセス権 |
|
|
アクセス権 |
open access |
|
アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 作成者 |
Tamura, Taku
Arai, Seisuke
Nagaya, Hisao
Mizuguchi, Jun
Wada, Ikuo
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| 内容記述 |
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内容記述タイプ |
Abstract |
|
内容記述 |
The endoplasmic reticulum (ER) plays essential roles in protein folding and assembly of secretory proteins. ER-resident molecular chaperones and related enzymes assist in protein maturation by co-operated interactions and modifications. However, the folding/assembly of multimeric proteins is not well understood. Here, we show that the maturation of fibrinogen, a hexameric secretory protein (two trimers from a, b and c subunits), occurs in a stepwise manner. The ac complex, a precursor for the trimer, is retained in the ER by lectin-like chaperones, and the b subunit is incorporated into the ac complex immediately after translation. ERp57, a protein disulfide isomerase homologue, is involved in the hexamer formation from two trimers. Our results indicate that the fibrinogen hexamer is formed sequentially, rather than simultaneously, using kinetic pause by lectin chaperones. This study provides a novel insight into the assembly of most abundant multi-subunit secretory proteins. |
|
言語 |
en |
| 出版タイプ |
|
|
出版タイプ |
VoR |
|
出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| 書誌情報 |
PLoS ONE
巻 8,
号 9,
p. e74580,
発行日 2013
|
| 収録物識別子 |
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|
収録物識別子タイプ |
ISSN |
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収録物識別子 |
1932-6203 |
| 出版者 |
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出版者 |
PLoS |
| 関連情報 |
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関連タイプ |
isIdenticalTo |
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識別子タイプ |
DOI |
|
|
関連識別子 |
https://doi.org/10.1371/journal.pone.0074580 |
| 権利情報 |
|
|
権利情報 |
©2013 Tamura et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
riA_2021_10 (5.3 MB)
