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Aurora B phosphorylates Bub1 to promote spindle assembly checkpoint signaling

View ORCID ProfileBabhrubahan Roy, View ORCID ProfileSimon J. Y. Han, Adrienne N. Fontan, Soubhagyalaxmi Jema, View ORCID ProfileAjit P. Joglekar
doi: https://doi.org/10.1101/2021.01.05.425459
Babhrubahan Roy
1Cell & Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Pl., Ann Arbor, MI-48109, USA
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Simon J. Y. Han
1Cell & Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Pl., Ann Arbor, MI-48109, USA
2Medical Scientist Training Program, University of Cincinnati College of Medicine, 3230 Eden Ave, Cincinnati, OH 45267, USA
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Adrienne N. Fontan
1Cell & Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Pl., Ann Arbor, MI-48109, USA
3Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, 455 Main St, Cambridge, MA 02142
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Soubhagyalaxmi Jema
1Cell & Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Pl., Ann Arbor, MI-48109, USA
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Ajit P. Joglekar
1Cell & Developmental Biology, University of Michigan Medical School, 109 Zina Pitcher Pl., Ann Arbor, MI-48109, USA
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  • For correspondence: ajitj@umich.edu
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Summary

Accurate chromosome segregation during cell division requires amphitelic chromosome attachment to the spindle apparatus. It is ensured by the combined activity of the Spindle Assembly Checkpoint1 (SAC), a signaling mechanism that delays anaphase onset in response to unattached chromosomes, and an error correction mechanism that eliminates syntelic attachments2. The SAC becomes active when Mps1 kinase sequentially phosphorylates the kinetochore protein Spc105/KNL1 and the signaling proteins that Spc105/KNL1 recruits to facilitate the production of the Mitotic Checkpoint Complex3-8 (MCC). The error correction mechanism is regulated by the Aurora B kinase, but Aurora B also promotes SAC signaling via indirect mechanisms9-12. Here we present evidence that Aurora B kinase activity directly promotes MCC production by working downstream of Mps1 in budding yeast and human cells. Using the ectopic SAC activation (eSAC) system, we find that the conditional dimerization of Aurora B in budding yeast, and an Aurora B recruitment domain in HeLa cells, with either Bub1 or Mad1, but not the phosphodomain of Spc105/KNL1, leads to ectopic MCC production and mitotic arrest13-16. Importantly, Bub1 must recruit both Mad1 and Cdc20 for this ectopic signaling activity. These and other data show that Aurora B cooperates with Bub1 to promote MCC production, but only after Mps1 licenses Bub1 recruitment to the kinetochore. This direct involvement of Aurora B in SAC signaling may maintain SAC signaling even after Mps1 activity in the kinetochore is lowered.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted October 24, 2021.
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Aurora B phosphorylates Bub1 to promote spindle assembly checkpoint signaling
Babhrubahan Roy, Simon J. Y. Han, Adrienne N. Fontan, Soubhagyalaxmi Jema, Ajit P. Joglekar
bioRxiv 2021.01.05.425459; doi: https://doi.org/10.1101/2021.01.05.425459
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Aurora B phosphorylates Bub1 to promote spindle assembly checkpoint signaling
Babhrubahan Roy, Simon J. Y. Han, Adrienne N. Fontan, Soubhagyalaxmi Jema, Ajit P. Joglekar
bioRxiv 2021.01.05.425459; doi: https://doi.org/10.1101/2021.01.05.425459

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