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

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 pi...

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Bibliographic Details
Published in:Cellular and molecular life sciences : CMLS 2010-06, Vol.67 (12), p.1957-1970
Main Authors: Park, Jung-Eun, Soung, Nak-Kyun, Johmura, Yoshikazu, Kang, Young H, Liao, Chenzhong, Lee, Kyung H, Park, Chi Hoon, Nicklaus, Marc C, Lee, Kyung S
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cell cycle
Cell Cycle Proteins - chemistry
Cell Cycle Proteins - metabolism
cell proliferation
Cellular biology
Humans
Kinases
Life Sciences
mitosis
Molecular biology
Phosphorylation
Plk1
Polo kinase
Polo-box domain
Polo-Like Kinase 1
Protein Kinases - chemistry
Protein Kinases - metabolism
Protein Serine-Threonine Kinases - chemistry
Protein Serine-Threonine Kinases - metabolism
Proto-Oncogene Proteins - chemistry
Proto-Oncogene Proteins - metabolism
Review
Substrates
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Summary: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.
ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-010-0279-9