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Molecular and Cellular Biology, January 2000, p. 286-298, Vol. 20, No. 1
0270-7306/0/$04.00+0

Essential Function of the Polo Box of Cdc5 in Subcellular Localization and Induction of Cytokinetic Structures

Sukgil Song,1 Tallessyn Z. Grenfell,2 Susan Garfield,3 Raymond L. Erikson,2 and Kyung S. Lee1,*

Laboratory of Metabolism1 and Laboratory of Experimental Carcinogenesis,3 Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, and Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 021382

Received 2 August 1999/Returned for modification 9 September 1999/Accepted 4 October 1999

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 C-terminal domain, termed the polo box. Here we show that the budding-yeast polo kinase Cdc5, when fused to green fluorescent protein and expressed under its endogenous promoter, localizes at spindle poles and the mother bud neck. Overexpression of Cdc5 can induce a class of cells with abnormally elongated buds in a polo box- and kinase activity-dependent manner. In addition to localizing at the spindle poles and cytokinetic neck filaments, Cdc5 induces and localizes to additional septin ring structures within the elongated buds. Without impairing kinase activity, conservative mutations in the polo box abolish the ability of Cdc5 to functionally complement the defect associated with a cdc5-1 temperature-sensitive mutation, to localize to the spindle poles and cytokinetic neck filaments, and to induce elongated cells with ectopic septin ring structures. Consistent with the polo box-dependent subcellular localization, the C-terminal domain of Cdc5, but not its polo box mutant, is sufficient for subcellular localization, and its overexpression appears to inhibit cytokinesis. These data provide evidence that the polo box is required to direct Cdc5 to specific subcellular locations and induce or organize cytokinetic structures.

* Corresponding author. Mailing address: Laboratory of Metabolism, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bldg. 37, Rm. 3D25, Bethesda, MD 20892. Phone: (301) 435-8894. Fax: (301) 496-8419. E-mail: kyunglee{at}pop.nci.nih.gov.

Molecular and Cellular Biology, January 2000, p. 286-298, Vol. 20, No. 1
0270-7306/0/$04.00+0


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