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Eukaryotic Cell, March 2008, p. 444-453, Vol. 7, No. 3
1535-9778/08/$08.00+0     doi:10.1128/EC.00283-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Requirement for the Budding Yeast Polo Kinase Cdc5 in Proper Microtubule Growth and Dynamics{triangledown} ,{dagger}

Chong J. Park,1,{ddagger} Jung-Eun Park,1,{ddagger} Tatiana S. Karpova,2 Nak-Kyun Soung,1 Li-Rong Yu,3 Sukgil Song,1 Kyung H. Lee,1 Xue Xia,4 Eugene Kang,1 Ilknur Dabanoglu,1 Doo-Yi Oh,1 James Y. Zhang,1 Young Hwi Kang,1 Stephen Wincovitch,5 Tim C. Huffaker,4 Timothy D. Veenstra,3 James G. McNally,2 and Kyung S. Lee1*

Laboratory of Metabolism,1 Laboratory of Receptor Biology and Gene Expression,2 Laboratory of Experimental Carcinogenesis, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892,5 Laboratory of Proteomics and Analytical Technologies, Advanced Technology Program, SAIC-Frederick, Inc., National Cancer Institute—Frederick, Frederick, Maryland 21702,3 Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 148534

Received 4 August 2007/ Accepted 16 December 2007

In many organisms, polo kinases appear to play multiple roles during M-phase progression. To provide new insights into the function of the budding yeast polo kinase Cdc5, we generated novel temperature-sensitive cdc5 mutants by mutagenizing the C-terminal noncatalytic polo box domain, a region that is critical for proper subcellular localization. One of these mutants, cdc5-11, exhibited a temperature-sensitive growth defect with an abnormal spindle morphology. Strikingly, provision of a moderate level of benomyl, a microtubule-depolymerizing drug, permitted cdc5-11 cells to grow significantly better than the isogenic CDC5 wild type in a FEAR (cdc Fourteen Early Anaphase Release)-independent manner. In addition, cdc5-11 required MAD2 for both cell growth and the benomyl-remedial phenotype. These results suggest that cdc5-11 is defective in proper spindle function. Consistent with this view, cdc5-11 exhibited abnormal spindle morphology, shorter spindle length, and delayed microtubule regrowth at the nonpermissive temperature. Overexpression of CDC5 moderately rescued the spc98-2 growth defect. Interestingly, both Cdc28 and Cdc5 were required for the proper modification of the spindle pole body components Nud1, Slk19, and Stu2 in vivo. They also phosphorylated these three proteins in vitro. Taken together, these observations suggest that concerted action of Cdc28 and Cdc5 on Nud1, Slk19, and Stu2 is important for proper spindle functions.

* Corresponding author. Mailing address: Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892. Phone: (301) 496-9635. Fax: (301) 496-8419. E-mail: kyunglee{at}mail.nih.gov

{triangledown} Published ahead of print on 4 January 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

{ddagger} C.J.P. and J.-E.P. contributed equally to this work.

Eukaryotic Cell, March 2008, p. 444-453, Vol. 7, No. 3
1535-9778/08/$08.00+0     doi:10.1128/EC.00283-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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