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Proteins interacting with CHFR, mitotic-checkpoint ubiquitin ligase
https://doi.org/10.15114/tr.41.23
https://doi.org/10.15114/tr.41.23155c03e3-072d-475c-9e95-38e1ef5a5636
名前 / ファイル | ライセンス | アクション |
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Item type | 紀要論文 / Departmental Bulletin Paper(1) | |||||
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公開日 | 2019-07-31 | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Proteins interacting with CHFR, mitotic-checkpoint ubiquitin ligase | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Ubiquitination | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Microtubule inhibitor | |||||
キーワード | ||||||
言語 | en | |||||
主題Scheme | Other | |||||
主題 | Cell cycle | |||||
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 | departmental bulletin paper | |||||
ID登録 | ||||||
ID登録 | 10.15114/tr.41.23 | |||||
ID登録タイプ | JaLC | |||||
著者 |
Mita, Hiroaki
× Mita, Hiroaki× Toyota, Minoru× Sasaki, Yasushi× Suzuki, Hiromu× Idogawa, Masashi× Kashima, Lisa× Tokino, Takashi |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Cell cycle progression is monitored by checkpoint mechanisms to ensure the integrity of the genome. CHFR which contains a RING domain and has ubiquitin ligase activity, a novel mitotic checkpoint gene, delays chromosome condensation in cells treated with microtubule poisons. CHFR is inactivated by promoter methylation and point mutations in various human tumors, and cancer cells lacking CHFR are sensitive to microtubule inhibitors. However, few reports are available on the molecular mechanism that accounts for the link between the sensitivity of cancer cells to microtubule inhibitors and the physiological function of CHFR. In the present study, we isolated cellular proteins capable of interacting with CHFR using yeast two-hybrid method to clarify the function of CHFR. As a result of the screening, we isolated canonical and noncanonical E2 ubiquitin conjugating enzymes as CHFR interacting proteins, which are involved in proteolytic and non-proteolytic ubiquitination respectively. This raises the possibility that CHFR is switching canonical and noncanonical ubiquitination depending on the situation of cells. On the other hand, we isolated gadd34 which interacted with the FHA domain of CHFR by two-hybrid screen. Coexpression in mammalian cells showed that gadd34 interacted with the FHA domain of CHFR, but gadd34 is not the substrate for CHFR, rather it promoted autoubiquitination of CHFR. Furthermore, CHFR moved, in part, from nucleus to cytoplasm in the presence of microtubule inhibitor docetaxel, which enabled colocalization of CHFR and gadd34 in cytoplasm. This colocalization was followed by cell death. These findings suggest that gadd34 and CHFR cooperate to mediate cell death in response to mitotic stress. | |||||
書誌情報 |
Tumor Research en : Tumor Research 巻 41, p. 23-41, 発行日 2006 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0041-4093 | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
出版者 | ||||||
出版者 | Sapporo Medical University |