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Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation

  1. Author:
    Kang, Y. H.
    Park, J. E.
    Yu, L. R.
    Soung, N. K.
    Yun, S. M.
    Bang, J. K.
    Seong, Y. S.
    Yu, H. T.
    Garfield, S.
    Veenstra, T. D.
    Lee, K. S.

  2. Author Address

    NCI, Lab Metab, Ctr Canc Res, Bethesda, MD 20892 USA. NCI, Cell Biol Lab, Ctr Canc Res, Bethesda, MD 20892 USA. NCI, Expt Carcinogenesis Lab, Ctr Canc Res, Bethesda, MD 20892 USA. NCI, Lab Proteom & Analyt Technol, Frederick, MD 21702 USA. Dankook Univ, Coll Med, Dept Biochem, Chunan 330714, South Korea. Univ Texas, SW Med Ctr, Dept Pharmacol, Dallas, TX 75390 USA.;Lee, KS, NCI, Lab Metab, Ctr Canc Res, Bethesda, MD 20892 USA.;kyunglee@mail.nih.gov
    1. Year: 2006
    2. Date: Nov
  2. Journal: Molecular Cell
    1. 24
    2. 3
    3. Pages: 409-422
  4. Type of Article: Article
  5. ISSN: 1097-2765
  1. Abstract:

    The polo-box domain (PBD) of mammalian polo-like kinase 1 (Plk1) is essential in targeting its catalytic activity to specific subcellular structures critical for mitosis. The mechanism underlying Plk1 recruitment to the kinetochores and the role of Plk1 at this site remain elusive. Here, we demonstrate that a PBD-binding protein, PBIP1, is crucial for recruiting Plk1 to the interphase and mitotic kinetochores. Unprecedentedly, Plk1 phosphorylated PBIP1 at T78, creating a self-tethering site that specifically interacted with the PBD of Plk1, but not Plk2 or Plk3. Later in mitosis, Plk1 also induced PBIP1 degradation in a T78-dependent manner, thereby enabling itself to interact with other components critical for proper kinetochore functions. Absence of the p-T78-dependent Plk1 localization induced a chromosome congression defect and compromised the spindle checkpoint, ultimately leading to aneuploidy. Thus, Plk1 self-regulates the Plk1-PBIP1 interaction to timely localize to the kinetochores and promote proper chromosome segregation.

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External Sources

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  2. DOI: 10.1016/j.molcel.2006.10.016
  3. View record in Web of Science®
  4. WOS: 000241869500008

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