Journal
JOURNAL OF CELL BIOLOGY
Volume 219, Issue 2, Pages -Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201907092
Keywords
-
Categories
Funding
- National Key Research and Development Program of China [2017YFA0503600]
- National Natural Science Foundation of China [31771499, 31571393, 31322032, 31371359, 31561130155, 81702552]
- Natural Science Foundation of Zhejiang Province [LZ19C070001]
- Royal Society Newton Advanced Fellowship [NA140075]
- Fundamental Research Funds for the Central Universities in China [2014XZZX003-35, 2019QNA7035]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available