Nature Cell Biology 8, 180 - 187 (2005)
Published online: 25 December 2005; | doi:10.1038/ncb1350
There is an Erratum (February 2006) associated with this Letter.
Complex formation of Plk1 and INCENP required for metaphase–anaphase transitionHidemasa Goto1, Tohru Kiyono2, Yasuko Tomono3, Aie Kawajiri1, Takeshi Urano4, Koichi Furukawa4, Erich A. Nigg5
& Masaki Inagaki11
Division of Biochemistry, Aichi Cancer Center Research Institute, Nagoya, Aichi 464-8681, Japan. 2
Virology Division, National Cancer Center Research Institute, Chuo-ku, Tokyo 104-0045, Japan. 3
Division of Molecular and Cell Biology, Shigei Medical Research Institute, Okayama, Okayama 701-0202, Japan. 4
Department of Biochemistry II, Nagoya University Graduate School of Medicine, Nagoya, Aichi 466-8550, Japan. 5
Department of Cell Biology, Max-Planck Institute for Biochemistry, D-82152 Martinstried, Germany.
Correspondence should be addressed to Masaki Inagaki minagaki@aichi-cc.jp Mitotic chromosomal dynamics is regulated by the coordinated activities of many mitotic kinases1, such as cyclin-dependent kinase 1 (Cdk1)2,
3, Aurora-B4 or Polo-like kinase 1 (Plk1)5, but the mechanisms of their coordination remain unknown. Here, we report that Cdk1 phosphorylates Thr 59 and Thr 388 on inner centromere protein (INCENP), which regulates the localization4 and kinase activity6,
7,
8 of Aurora-B from prophase to metaphase. INCENP depletion disrupts Plk1 localization specifically at the kinetochore. This phenotype is rescued by the exogenous expression of INCENP wild type and INCENP mutated at Thr 59 to Ala (T59A), but not at Thr 388 to Ala (T388A). The replacement of endogenous INCENP with T388A resulted in the delay of progression from metaphase to anaphase. We propose that INCENP phosphorylation by Cdk1 is necessary for the recruitment of Plk1 to the kinetochore, and that the complex formation of Plk1 and Aurora-B on INCENP may play crucial roles in the regulation of chromosomal dynamics.
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