2019年12月2日
CDK1-mediated CENP-C phosphorylation modulates CENP-A binding and mitotic kinetochore localization.
The Journal of cell biology
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- 巻
- 218
- 号
- 12
- 開始ページ
- 4042
- 終了ページ
- 4062
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1083/jcb.201907006
- 出版者・発行元
- Rockefeller University Press
The kinetochore is essential for faithful chromosome segregation during mitosis. To form a functional kinetochore, constitutive centromere-associated network (CCAN) proteins are assembled on the centromere chromatin that contains the centromere-specific histone CENP-A. CENP-C, a CCAN protein, directly interacts with the CENP-A nucleosome to nucleate the kinetochore structure. As CENP-C is a hub protein for kinetochore assembly, it is critical to address how the CENP-A-CENP-C interaction is regulated during cell cycle progression. To address this question, we investigated the CENP-C C-terminal region, including a conserved CENP-A-binding motif, in both chicken and human cells and found that CDK1-mediated phosphorylation of CENP-C facilitates its binding to CENP-A in vitro and in vivo. We observed that CENP-A binding is involved in CENP-C kinetochore localization during mitosis. We also demonstrate that the CENP-A-CENP-C interaction is critical for long-term viability in human RPE-1 cells. These results provide deeper insights into protein-interaction network plasticity in centromere proteins during cell cycle progression.
- リンク情報
- ID情報
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- DOI : 10.1083/jcb.201907006
- ORCIDのPut Code : 63993788
- PubMed ID : 31676716
- PubMed Central 記事ID : PMC6891089