Phosphorylation of EB2 by Aurora B and CDK1 ensures mitotic progression and genome stability

Makoto Iimori, Sugiko Watanabe, Shinichi Kiyonari, Kazuaki Matsuoka, Ryo Sakasai, Hiroshi Saeki, Eiji Oki, Hiroyuki Kitao, Yoshihiko Maehara

研究成果: ジャーナルへの寄稿記事

12 引用 (Scopus)

抜粋

Temporal regulation of microtubule dynamics is essential for proper progression of mitosis and control of microtubule plus-end tracking proteins by phosphorylation is an essential component of this regulation. Here we show that Aurora B and CDK1 phosphorylate microtubule end-binding protein 2 (EB2) at multiple sites within the amino terminus and a cluster of serine/threonine residues in the linker connecting the calponin homology and end-binding homology domains. EB2 phosphorylation, which is strictly associated with mitotic entry and progression, reduces the binding affinity of EB2 for microtubules. Expression of non-phosphorylatable EB2 induces stable kinetochore microtubule dynamics and delays formation of bipolar metaphase plates in a microtubule binding-dependent manner, and leads to aneuploidy even in unperturbed mitosis. We propose that Aurora B and CDK1 temporally regulate the binding affinity of EB2 for microtubules, thereby ensuring kinetochore microtubule dynamics, proper mitotic progression and genome stability.

元の言語英語
記事番号11117
ジャーナルNature communications
7
DOI
出版物ステータス出版済み - 3 31 2016

    フィンガープリント

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

これを引用

Iimori, M., Watanabe, S., Kiyonari, S., Matsuoka, K., Sakasai, R., Saeki, H., ... Maehara, Y. (2016). Phosphorylation of EB2 by Aurora B and CDK1 ensures mitotic progression and genome stability. Nature communications, 7, [11117]. https://doi.org/10.1038/ncomms11117