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Cell Cycle. 2008 Jan 15;7(2):141-5. Epub 2007 Oct 16.

Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: self- versus non-self-priming.

Author information

1
Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-4258, USA. kyunglee@mail.nih.gov

Abstract

Mammalian polo-like kinase 1 (Plk1) has been studied intensively as a key element in regulating diverse mitotic events during M-phase progression. Plk1 is spatially regulated through the targeting activity of the conserved polo-box domain (PBD) present in the C-terminal non-catalytic region. Over the years, studies have demonstrated that the PBD forms a phospho-epitope binding module and the PBD-dependent interaction is critical for proper subcellular localization of Plk1. The current prevailing model is that the PBD binds to a phospho-epitope generated by Cdc2 or other Pro-directed kinases. Here we discuss a recent finding that Plk1 also self-promotes its localization by generating its own PBD-docking site.

PMID:
18216497
DOI:
10.4161/cc.7.2.5272
[Indexed for MEDLINE]

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