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Polo-box domain: a versatile mediator of polo-like kinase function

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Abstract

Members of the polo subfamily of protein kinases have emerged as important regulators in diverse aspects of the cell cycle and cell proliferation. A large body of evidence suggests that a highly conserved polo-box domain (PBD) present in the C-terminal non-catalytic region of polo kinases plays a pivotal role in the function of these enzymes. Recent advances in our comprehension of the mechanisms underlying mammalian polo-like kinase 1 (Plk1)-dependent protein–protein interactions revealed that the PBD serves as an essential molecular mediator that brings the kinase domain of Plk1 into proximity with its substrates, mainly through phospho-dependent interactions with its target proteins. In this review, current understanding of the structure and functions of PBD, mode of PBD-dependent interactions and substrate phosphorylation, and other phospho-independent functions of PBD are discussed.

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Acknowledgments

We are grateful to the present and past members of our laboratory for their great work and stimulating discussions, and to many colleagues for generously sharing their views and insights. We apologize to all authors whose work could not be cited due to space limitations.

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Authors and Affiliations

  1. Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bldg. 37, Rm. 3118, Bethesda, MD, 20892-4258, USA

    Jung-Eun Park, Nak-Kyun Soung, Yoshikazu Johmura, Young H. Kang, Kyung H. Lee, Chi Hoon Park & Kyung S. Lee

  2. Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, National Institutes of Health, Frederick, MD, 21702, USA

    Chenzhong Liao & Marc C. Nicklaus

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  1. Jung-Eun Park
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  2. Nak-Kyun Soung
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Correspondence to Kyung S. Lee.

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Park, JE., Soung, NK., Johmura, Y. et al. Polo-box domain: a versatile mediator of polo-like kinase function. Cell. Mol. Life Sci. 67, 1957–1970 (2010). https://doi.org/10.1007/s00018-010-0279-9

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  • DOI: https://doi.org/10.1007/s00018-010-0279-9

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