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Integration of kinase and phosphatase activities by BUBR1 ensures formation of stable kinetochore-microtubule attachments.

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Affiliations

  • 1. Molecular Cancer Research and Cancer Genomics Centre, UMC Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands.
      Authors
    • Suijkerbuijk SJ 1
    (1 author)

ORCIDs linked to this article

Developmental Cell, 01 Oct 2012, 23(4):745-755
https://doi.org/10.1016/j.devcel.2012.09.005 PMID: 23079597 

Abstract 

Maintenance of chromosomal stability depends on error-free chromosome segregation. The pseudokinase BUBR1 is essential for this, because it is a core component of the mitotic checkpoint and is required for formation of stable kinetochore-microtubule attachments. We have identified a conserved and highly phosphorylated domain (KARD) in BUBR1 that is crucial for formation of kinetochore-microtubule attachments. Deletion of this domain or prevention of its phosphorylation abolishes formation of kinetochore microtubules, which can be reverted by inhibiting Aurora B activity. Phosphorylation of KARD by PLK1 promotes direct interaction of BUBR1 with the PP2A-B56α phosphatase that counters excessive Aurora B activity at kinetochores. As a result, removal of BUBR1 from mitotic cells or inhibition of PLK1 reduces PP2A-B56α kinetochore binding and elevates phosphorylation of Aurora B substrates on the outer kinetochore. We propose that PLK1 and BUBR1 cooperate to stabilize kinetochore-microtubule interactions by regulating PP2A-B56α-mediated dephosphorylation of Aurora B substrates at the kinetochore-microtubule interface.

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Read article at publisher's site: https://doi.org/10.1016/j.devcel.2012.09.005

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European Research Council (1)