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Published online March 31, 2008
doi:10.1083/jcb.200712027
The Journal of Cell Biology, Vol. 181, No. 1, 65-78
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Seki et al.
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Article

 Plk1- and β-TrCP–dependent degradation of Bora controls mitotic progression

Akiko Seki1, Judith A. Coppinger2, Haining Du1, Chang-Young Jang1, John R. Yates, III2, and Guowei Fang1

1 Department of Biological Sciences, Stanford University, Stanford, CA 94305
2 Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037

Correspondence to Guowei Fang: gwfang{at}stanford.edu

Through a convergence of functional genomic and proteomic studies, we identify Bora as a previously unknown cell cycle protein that interacts with the Plk1 kinase and the SCF–β-TrCP ubiquitin ligase. We show that the Bora protein peaks in G2 and is degraded by proteasomes in mitosis. Proteolysis of Bora requires the Plk1 kinase activity and is mediated by SCF–β-TrCP. Plk1 phosphorylates a conserved DSGxxT degron in Bora and promotes its interaction with β-TrCP. Mutations in this degron stabilize Bora. Expression of a nondegradable Bora variant prolongs the metaphase and delays anaphase onset, indicating a physiological requirement of Bora degradation. Interestingly, the activity of Bora is also required for normal mitotic progression, as knockdown of Bora activates the spindle checkpoint and delays sister chromatid segregation. Mechanistically, Bora regulates spindle stability and microtubule polymerization and promotes tension across sister kinetochores during mitosis. We conclude that tight regulation of the Bora protein by its synthesis and degradation is critical for cell cycle progression.

Abbreviations used in this paper: PBD, polo-box domain; Plk, polo-like kinase.


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