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

Kyung S. Lee, Jung-Eun Park, Young Hwi Kang, Wendy Zimmerman, Nak-Kyun Soung, Yeon-Sun Seong, Sahng-June Kwak and Raymond L. Erikson

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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.

Authors

Kyung S. Lee

National Cancer Institute; Bethesda, MD

Jung-Eun Park

National Cancer Institute; Bethesda, MD

Young Hwi Kang

National Cancer Institute; Bethesda, MD

Wendy Zimmerman

Harvard University; Cambridge, MA

Nak-Kyun Soung

National Cancer Institute; Bethesda, MD

Yeon-Sun Seong

Dankook University; Chunan, South Korea

Sahng-June Kwak

Dankook University; Chunan, South Korea

Raymond L. Erikson

Harvard University; Cambridge, MA

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If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.