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Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation

  1. Author:
    Feng, Y.
    Yuan, J. H.
    Maloid, S. C.
    Fisher, R.
    Copeland, T. D.
    Longo, D. L.
    Conrads, T. P.
    Veenstra, T. D.
    Ferris, A.
    Hughes, S.
    Dimitrov, D. S.
    Ferris, D. K.

  2. Author Address

    NCI, Lab Canc Prevent, Frederick, MD 21701 USA. NCI, Basic Res Program, SAIC Federick Inc, Frederick, MD 21701 USA. NCI, Nanobiol Program, CCR, Frederick, MD 21701 USA. NCI, Mass Spectrometry Ctr, SAIC Federick Inc, Frederick, MD 21701 USA. NCI, Retroviral Replicat Lab, HIV Drug Resistance Program, Frederick, MD 21701 USA. NIA, Baltimore, MD 21224 USA.;Feng, Y, NCI, Lab Canc Prevent, Frederick, MD 21701 USA.;yfeng@mail.ncifcrf.gov
    1. Year: 2006
    2. Date: Oct
  2. Journal: Biochemical and Biophysical Research Communications
    1. 349
    2. 1
    3. Pages: 144-152
  4. Type of Article: Article
  5. ISSN: 0006-291X
  1. Abstract:

    Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1. Plk1 is capable of phosphorylating co-immunoprecipitated Ran in vitro on serine-135 and Ran is phosphorylated in vivo at the same site during mitosis when Plk1 is normally activated. Cell cultures over-expressing a Ran S135D mutant have significantly higher numbers of abnormal mitotic cells than those over-expressing either wild-type or S135A Ran. The abnormalities in S135D mutant cells are similar to cells over-expressing Plk1. Our data suggests that Ran is a physiological substrate of Plk1 and that Plk1 regulates the spindle organization partially through its phosphorylation on Ran. Published by Elsevier Inc.

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  2. DOI: 10.1016/j.bbrc.2006.08.028
  3. View record in Web of Science®
  4. WOS: 000240650000019

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