Aurora B kinase plays an essential role in chromosome bi-orientation, which is a prerequisite for equal segregation of chromosomes during mitosis. However, it remains largely unclear whether centromere-localized Aurora B is required for faithful chromosome segregation. Here we show that histone H3 Thr-3 phosphorylation (H3pT3) and H2A Thr-120 phosphorylation (H2ApT120) can independently recruit Aurora B. Disrupting H3pT3-mediated localization of Aurora B at the inner centromere impedes the decline in H2ApT120 during metaphase and causes H2ApT120-dependent accumulation of Aurora B at the kinetochore-proximal centromere. Consequently, silencing of the spindle assembly checkpoint (SAC) is delayed, whereas the fidelity of chromosome segregation is negligibly affected. Further eliminating an H2ApT120-dependent pool of Aurora B restores proper timing for SAC silencing but increases chromosome missegregation. Our data indicate that H2ApT120-mediated localization of Aurora B compensates for the loss of an H3pT3-dependent pool of Aurora B to correct improper kinetochore–microtubule attachments. This study provides important insights into how centromeric Aurora B regulates SAC and kinetochore attachment to microtubules to ensure error-free chromosome segregation.
Centromere-localized Aurora B kinase is required for the fidelity of chromosome segregation
C. Liang and Z. Zhang contributed equally to this paper.
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Cai Liang, Zhenlei Zhang, Qinfu Chen, Haiyan Yan, Miao Zhang, Linli Zhou, Junfen Xu, Weiguo Lu, Fangwei Wang; Centromere-localized Aurora B kinase is required for the fidelity of chromosome segregation. J Cell Biol 3 February 2020; 219 (2): e201907092. doi: https://doi.org/10.1083/jcb.201907092
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