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タイトル: Stress-activated mitogen-activated protein kinases c-Jun NH 2-terminal kinase and p38 target Cdc25B for degradation
著者: Uchida, Sanae
Yoshioka, Katsuji link image link image
Kizu, Ryoichi link image
Nakagama, Hitoshi
Matsunaga, Tsukasa link image link image
Ishizaka, Yukihito
Poon, Randy Y. C.
Yamashita, Katsumi link image link image
内田, 早苗
善岡, 克次
松永, 司
山下, 克美
発行日: 2009年 8月15日
出版社(者): American Association for Cancer Research
雑誌名: Cancer Research
ISSN: 0008-5472
巻: 69
号: 16
開始ページ: 6438
終了ページ: 6444
抄録: 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.
DOI: 10.1158/0008-5472.CAN-09-0869
URI: http://hdl.handle.net/2297/19420
資料種別: Journal Article
版表示: author

このアイテムを引用あるいはリンクする場合は次の識別子を使用してください。 http://hdl.handle.net/2297/19420



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