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Stress-activated mitogen-activated protein kinases c-Jun NH 2-terminal kinase and p38 target Cdc25B for degradation
http://hdl.handle.net/2297/19420
http://hdl.handle.net/2297/19420eff8e376-1d7c-4d80-9244-31518a101f69
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
PH-PR-YAMASHITA-K-6438.pdf (725.9 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-10-04 | |||||
| タイトル | ||||||
| タイトル | Stress-activated mitogen-activated protein kinases c-Jun NH 2-terminal kinase and p38 target Cdc25B for degradation | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 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 | |||||
| 著者 |
Uchida, Sanae
× Uchida, Sanae× Yoshioka, Katsuji× Kizu, Ryoichi× Nakagama, Hitoshi× Matsunaga, Tsukasa× Ishizaka, Yukihito× Poon, Randy Y. C.× Yamashita, Katsumi |
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| 提供者所属 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 金沢大学医薬保健研究域薬学系 | |||||
| 書誌情報 |
Cancer Research 巻 69, 号 16, p. 6438-6444, 発行日 2009-08-15 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0008-5472 | |||||
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| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA00598557 | |||||
| DOI | ||||||
| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1158/0008-5472.CAN-09-0869 | |||||
| 出版者 | ||||||
| 出版者 | American Association for Cancer Research | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Cdc25 dual specificity phosphatases positively regulate the cell cycle by activating cyclin-dependent kinase/cyclin complexes. Of the three mammalian Cdc25 isoforms, Cdc25A is phosphorylated by genotoxic stress-activated Chk1 or Chk2, which triggers its SCFβ-TrCP-mediated degradation. However, the roles of Cdc25B and Cdc25C in cell stress checkpoints remain inconclusive. We herein report that c-Jun NH2-terminal kinase (JNK) induces the degradation of Cdc25B. Nongenotoxic stress induced by anisomycin caused rapid degradation of Cdc25B as well as Cdc25A. Cdc25B degradation was dependent mainly on JNK and partially on p38 mitogen-activated protein kinase (p38). Accordingly, cotransfection with JNK1, JNK2, or p38 destabilized Cdc25B. In vitro kinase assays and site-directed mutagenesis experiments revealed that the critical JNK and p38 phosphorylation site in Cdc25B was Ser101. Cdc25B with Ser101 mutated to alanine was refractory to anisomycin-induced degradation, and cells expressing such mutant Cdc25B proteins were able to override the anisomycin-induced G2 arrest. These results highlight the importance of a novel JNK/p38-Cdc25B axis for a nongenotoxic stress-induced cell cycle checkpoint. ©2009 American Association for Cancer Research. | |||||
| 著者版フラグ | ||||||
| 出版タイプ | AM | |||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
