| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2023-02-19 |
| タイトル |
|
|
タイトル |
The activation mechanism of the aryl hydrocarbon receptor (AhR) by molecular chaperone HSP90 |
|
言語 |
en |
| 言語 |
|
|
言語 |
eng |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
AhR |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
Aryl hydrocarbon receptor |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
Dioxin receptor |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
HSP90 |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
Molecular chaperone |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
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 |
Tsuji, Noriko
Fukuda, Kana
Nagata, Yuhtaroh
Okada, Hirotaka
Haga, Asami
Hatakeyama, Shiori
Yoshida, Shiho
Okamoto, Tomoya
Hosaka, Miki
Sekine, Kazuhiro
Ohtaka, Kei
Yamamoto, Soh
Otaka, Michiro
Grave, Ewa
Itoh, Hideaki
|
| 内容記述 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
The aryl hydrocarbon receptor is a member of the nuclear receptor superfamily that associates with the molecular chaperone HSP90 in the cytoplasm. The activation mechanism of the AhR is not yet fully understood. It has been proposed that after binding of ligands such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), 3methylcholanthrene (3-MC), or β-naphthoflavone (β-NF), the AhR dissociates from HSP90 and translocates to the nucleus. It has also been hypothesized that the AhR translocates to the nucleus and forms a complex with HSP90 and other co-chaperones. There are a few reports about the direct association or dissociation of AhR and HSP90 due to difficulties in purifying AhR. We constructed and purified the PAS domain from AhR. Binding of the AhR-PAS domain to β-NF affinity resin suggested that it possesses ligand-binding affinity. We demonstrated that the AhR-PAS domain binds to HSP90 and the association is not affected by ligand binding. The ligand 17-DMAG inhibited binding of HSP90 to GST-PAS. In an immunoprecipitation assay, HSP90 was co-immunoprecipitated with AhR both in the presence or absence of ligand. Endogenous AhR decreased in the cytoplasm and increased in the nucleus of HeLa cells 15. min after treatment with ligand. These results suggested that the ligand-bound AhR is translocated to nucleus while in complex with HSP90.We used an in situ proximity ligation assay to confirm whether AhR was translocated to the nucleus alone or together with HSP90. HSP90 was co-localized with AhR after the nuclear translocation. It has been suggested that the ligand-bound AhR was translocated to the nucleus with HSP90. Activated AhR acts as a transcription factor, as shown by the transcription induction of the gene CYP1A1 8. h after treatment with β-NF. |
|
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 |
en : FEBS Open Bio
巻 4,
号 1,
p. 796-803,
発行日 2014
|
| 収録物識別子 |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
2211-5463 |
| 出版者 |
|
|
出版者 |
Elsevier |
| 関連情報 |
|
|
関連タイプ |
isIdenticalTo |
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
https://doi.org/10.1016/j.fob.2014.09.003 |
| 権利情報 |
|
|
権利情報 |
© 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/) |
riA_2022_11.pdf (1.3 MB)
