4.6 Article

Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: Self-priming

Journal

CELL CYCLE
Volume 7, Issue 2, Pages 141-145

Publisher

LANDES BIOSCIENCE
DOI: 10.4161/cc.7.2.5272

Keywords

polo kinase; polo-box domain; self-priming; non-self-priming

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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.

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