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https://hdl.handle.net/20.500.14094/90007688
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2024-04-26
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90007688 (fulltext)
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メタデータID
90007688
アクセス権
open access
出版タイプ
Version of Record
タイトル
Functional impacts of the ubiquitin-proteasome system on DNA damage recognition in global genome nucleotide excision repair
著者
Sakai, Wataru ; Yuasa-Sunagawa, Mayumi ; Kusakabe, Masayuki ; Kishimoto, Aiko ; Matsui, Takeshi ; Kaneko, Yuki ; Akagi, Jun-ichi ; Huyghe, Nicolas ; Ikura, Masae ; Ikura, Tsuyoshi ; Hanaoka, Fumio ; Yokoi, Masayuki ; Sugasawa, Kaoru
著者ID
A1289
研究者ID
1000070526251
KUID
https://kuid-rm-web.ofc.kobe-u.ac.jp/search/detail?systemId=3d25cd9ab339d672520e17560c007669
著者名
Sakai, Wataru
酒井, 恒
サカイ, ワタル
所属機関名
バイオシグナル総合研究センター
著者名
Yuasa-Sunagawa, Mayumi
著者ID
A2109
KUID
https://kuid-rm-web.ofc.kobe-u.ac.jp/search/detail?systemId=15bfd3363269d07a520e17560c007669
著者名
Kusakabe, Masayuki
日下部, 将之
クサカベ, マサユキ
所属機関名
バイオシグナル総合研究センター
著者名
Kishimoto, Aiko
著者名
Matsui, Takeshi
著者名
Kaneko, Yuki
著者名
Akagi, Jun-ichi
著者名
Huyghe, Nicolas
著者名
Ikura, Masae
著者名
Ikura, Tsuyoshi
著者名
Hanaoka, Fumio
著者ID
A0500
研究者ID
1000000322701
KUID
https://kuid-rm-web.ofc.kobe-u.ac.jp/search/detail?systemId=880c30d5cc97a406520e17560c007669
著者名
Yokoi, Masayuki
横井, 雅幸
ヨコイ, マサユキ
所属機関名
バイオシグナル総合研究センター
著者ID
A1240
研究者ID
1000070202124
KUID
https://kuid-rm-web.ofc.kobe-u.ac.jp/search/detail?systemId=a37ee6502e5cceaa520e17560c007669
著者名
Sugasawa, Kaoru
菅澤, 薫
スガサワ, カオル
所属機関名
バイオシグナル総合研究センター
収録物名
Scientific Reports
巻(号)
10(1)
ページ
19704-19704
出版者
Nature Research
刊行日
2020-11-12
公開日
2020-12-16
抄録
The ubiquitin-proteasome system (UPS) plays crucial roles in regulation of various biological processes, including DNA repair. In mammalian global genome nucleotide excision repair (GG-NER), activation of the DDB2-associated ubiquitin ligase upon UV-induced DNA damage is necessary for efficient recognition of lesions. To date, however, the precise roles of UPS in GG-NER remain incompletely understood. Here, we show that the proteasome subunit PSMD14 and the UPS shuttle factor RAD23B can be recruited to sites with UV-induced photolesions even in the absence of XPC, suggesting that proteolysis occurs at DNA damage sites. Unexpectedly, sustained inhibition of proteasome activity results in aggregation of PSMD14 (presumably with other proteasome components) at the periphery of nucleoli, by which DDB2 is immobilized and sequestered from its lesion recognition functions. Although depletion of PSMD14 alleviates such DDB2 immobilization induced by proteasome inhibitors, recruitment of DDB2 to DNA damage sites is then severely compromised in the absence of PSMD14. Because all of these proteasome dysfunctions selectively impair removal of cyclobutane pyrimidine dimers, but not (6-4) photoproducts, our results indicate that the functional integrity of the proteasome is essential for the DDB2-mediated lesion recognition sub-pathway, but not for GG-NER initiated through direct lesion recognition by XPC.
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バイオシグナル総合研究センター
学術雑誌論文
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© The Author(s) 2020.
This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
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資源タイプ
journal article
言語
English (英語)
eISSN
2045-2322
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関連情報
DOI
https://doi.org/10.1038/s41598-020-76898-2
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