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Plk1- and beta-TrCP-dependent degradation of Bora controls mitotic progression

Academic Article
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Overview

authors

  • Seki, A.
  • Coppinger, J. A.
  • Du, H.
  • Jang, C. Y.
  • Yates III, John
  • Fang, G.

publication date

  • April 2008

journal

  • Journal of Cell Biology  Journal

abstract

  • 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-beta-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-beta-TrCP. Plk1 phosphorylates a conserved DSGxxT degron in Bora and promotes its interaction with beta-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.

subject areas

  • Amino Acid Motifs
  • Cell Cycle
  • Cell Cycle Proteins
  • HeLa Cells
  • Humans
  • Mitosis
  • Proteasome Endopeptidase Complex
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins
  • Ubiquitination
  • beta-Transducin Repeat-Containing Proteins
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Identity

PubMed Central ID

  • PMC2287288

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.200712027

PubMed ID

  • 18378770
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Additional Document Info

start page

  • 65

end page

  • 78

volume

  • 181

issue

  • 1

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