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DOI | 10.1038/ncomms14598 |
Cdk1-mediated DIAPH1 phosphorylation maintains metaphase cortical tension and inactivates the spindle assembly checkpoint at anaphase | |
Nishimura, Koutarou1; Johmura, Yoshikazu1,2; Deguchi, Katashi3; Jiang, Zixian3; Uchida, Kazuhiko S. K.4; Suzuki, Narumi2; Shimada, Midori5; Chiba, Yoshie2; Hirota, Toru4; Yoshimura, Shige H.3; Kono, Keiko1,6; Nakanishi, Makoto1,2 | |
2019-02-28 | |
发表期刊 | NATURE COMMUNICATIONS
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ISSN | 2041-1723 |
出版年 | 2019 |
卷号 | 10 |
文章类型 | Article |
语种 | 英语 |
国家 | Japan |
英文摘要 | Animal cells undergo rapid rounding during mitosis, ensuring proper chromosome segregation, during which an outward rounding force abruptly increases upon prometaphase entry and is maintained at a constant level during metaphase. Initial cortical tension is generated by the actomyosin system to which both myosin motors and actin network architecture contribute. However, how cortical tension is maintained and its physiological significance remain unknown. We demonstrate here that Cdk1-mediated phosphorylation of DIAPH1 stably maintains cortical tension after rounding and inactivates the spindle assembly checkpoint (SAC). Cdk1 phosphorylates DIAPH1, preventing profilin1 binding to maintain cortical tension. Mutation of DIAPH1 phosphorylation sites promotes cortical F-actin accumulation, increases cortical tension, and delays anaphase onset due to SAC activation. Measurement of the intrakinetochore length suggests that Cdk1-mediated cortex relaxation is indispensable for kinetochore stretching. We thus uncovered a previously unknown mechanism by which Cdk1 coordinates cortical tension maintenance and SAC inactivation at anaphase onset. |
领域 | 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000459899900001 |
WOS关键词 | CELL-SHAPE ; ACTIN ; DYNEIN ; RETRACTION ; MECHANISM ; PROTEINS ; RIGIDITY ; POSITION ; GROWTH ; FORMIN |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/203217 |
专题 | 资源环境科学 |
作者单位 | 1.Nagoya City Univ, Grad Sch Med Sci, Dept Cell Biol, Mizuho Ku, 1 Kawasumi,Mizuho Cho, Nagoya, Aichi 4678601, Japan; 2.Univ Tokyo, IMS, Div Canc Cell Biol, Minato Ku, 4-6-1 Shirokanedai, Tokyo 1088639, Japan; 3.Kyoto Univ, Grad Sch Biostudies, Sakyo Ku, Kyoto 6068501, Japan; 4.JFCR, Canc Inst, Tokyo 1358550, Japan; 5.Yamaguchi Univ, Joint Fac Vet Med, Yamaguchi 7538515, Japan; 6.Grad Univ, Okinawa Inst Sci & Technol, 1919-1 Tancha, Onna, Okinawa 9040495, Japan |
推荐引用方式 GB/T 7714 | Nishimura, Koutarou,Johmura, Yoshikazu,Deguchi, Katashi,et al. Cdk1-mediated DIAPH1 phosphorylation maintains metaphase cortical tension and inactivates the spindle assembly checkpoint at anaphase[J]. NATURE COMMUNICATIONS,2019,10. |
APA | Nishimura, Koutarou.,Johmura, Yoshikazu.,Deguchi, Katashi.,Jiang, Zixian.,Uchida, Kazuhiko S. K..,...&Nakanishi, Makoto.(2019).Cdk1-mediated DIAPH1 phosphorylation maintains metaphase cortical tension and inactivates the spindle assembly checkpoint at anaphase.NATURE COMMUNICATIONS,10. |
MLA | Nishimura, Koutarou,et al."Cdk1-mediated DIAPH1 phosphorylation maintains metaphase cortical tension and inactivates the spindle assembly checkpoint at anaphase".NATURE COMMUNICATIONS 10(2019). |
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