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

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)


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.

Original languageEnglish
Article number11117
JournalNature communications
Publication statusPublished - Mar 31 2016

All Science Journal Classification (ASJC) codes

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


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