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Mutation of the Polo-Box Disrupts Localization and Mitotic Functions of the Mammalian Polo Kinase PIK
Kyung S. Lee, Tallessyn Z. Grenfell, Frederic R. Yarm and Raymond L. Erikson
Proceedings of the National Academy of Sciences of the United States of America
Vol. 95, No. 16 (Aug. 4, 1998), pp. 9301-9306
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/45469
Page Count: 6
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Members of the polo subfamily of protein kinases play pivotal roles in cell proliferation. In addition to the kinase domain, polo kinases have a strikingly conserved sequence in the noncatalytic domain, termed the polo-box. The function of the polo-box is currently undefined. The mammalian polo-like kinase PIK is a functional homologue of Saccharomyces cerevisiae Cdc5. Here, we show that PIK localizes at the spindle poles and cytokinetic neck filaments. Without impairing kinase activity, a conservative mutation in the polo-box disrupts the capacity of PIK to complement the defect associated with a cdc5-1 temperature-sensitive mutation and to localize to these subcellular structures. Our data provide evidence that the polo-box plays a critical role in PIK function, likely by directing its subcellular localization.
Proceedings of the National Academy of Sciences of the United States of America © 1998 National Academy of Sciences