Polo-box domain: a versatile mediator of polo-like kinase function |
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Authors: | Jung-Eun Park Nak-Kyun Soung Yoshikazu Johmura Young H. Kang Chenzhong Liao Kyung H. Lee Chi Hoon Park Marc C. Nicklaus Kyung S. Lee |
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Affiliation: | (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;(2) Chemical Biology Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, National Institutes of Health, Frederick, MD 21702, USA; |
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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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