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MafB protein stability is regulated by the JNK and ubiquitin-proteasome pathways
https://doi.org/10.24517/00027526
https://doi.org/10.24517/000275266b27128c-13d8-486d-816b-00a98a7cbeb0
名前 / ファイル | ライセンス | アクション |
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CA-PR-YOSHIOKA-K-94.pdf (681.5 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2017-10-05 | |||||
タイトル | ||||||
タイトル | MafB protein stability is regulated by the JNK and ubiquitin-proteasome pathways | |||||
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 | |||||
ID登録 | ||||||
ID登録 | 10.24517/00027526 | |||||
ID登録タイプ | JaLC | |||||
著者 |
Tanahashi, Hiroshi
× Tanahashi, Hiroshi× Kito, Keiji× Ito, Takashi× Yoshioka, Katsuji |
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著者別表示 |
棚橋, 浩
× 棚橋, 浩× 紀藤 , 圭治× 伊藤, 隆司× 善岡, 克次 |
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提供者所属 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 金沢大学がん研究所がん分子細胞制御 | |||||
書誌情報 |
Archives of Biochemistry and Biophysics 巻 494, 号 1, p. 94-100, 発行日 2010-02-01 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0003-9861 | |||||
NCID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00547159 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1016/j.abb.2009.11.018 | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | MafB is a basic leucine zipper transcription factor that plays important roles in development and differentiation processes. During osteoclastogenesis, its expression is downregulated at the transcriptional level via the JNK and p38 MAP kinase pathways. In the present study, we demonstrated that MafB protein stability is regulated by JNK and identified a phosphorylation site, Thr62. The expression of a constitutively active form of JNK (a fusion protein MKK7α1-JNK1β1) promoted the degradation of MafB in COS7 cells, and a T62A substitution significantly reduced the instability of MafB. The introduction of a fourfold (T58A/T62A/S70A/S74A) substitution in an acidic transcription-activating domain almost protected the instability resulting from the activation of JNK. Furthermore, treatment with proteasome inhibitors increased the MafB level, and a high-molecular-weight smear, characteristic of polyubiquitination, was observed in lysates from cells in which MafB, ubiquitin, and MKK7α1-JNK1β1 were co-expressed. These results suggest that phosphorylation of MafB by JNK confers susceptibility to proteasomal degradation. © 2009 Elsevier Inc. All rights reserved. | |||||
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 |