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MBC in Press, published online ahead of print April 27, 2005
Mol. Biol. Cell 10.1091/mbc.E04-09-0769

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Submitted on September 3, 2004
Revised on April 7, 2005
Accepted on April 14, 2005

Roles of Pdk1p, a Fission Yeast Protein Related to Phosphoinositide-dependent Protein Kinase, in the Regulation of Mitosis and Cytokinesis

Andrea Bimbó,*{dagger} Jianhua Liu,{ddagger} and Mohan K. Balasubramanian*{dagger}

*Cell Division Laboratory, Temasek Life Sciences Laboratory and {dagger}Department of Biological Sciences, National University of Singapore, Singapore 117604, Singapore; {ddagger}Genome Institute of Singapore, Singapore 138672, Singapore

Monitoring Editor: David Drubin

Proteins related to the phosphoinosotide-dependent protein kinase family have been identified in the vast majority of eukaryotes. Although much is known about upstream mechanisms that regulate the PDK1-family of kinases in metazoans, how these kinases regulate cell growth and division remains unclear. Here we characterize a fission yeast protein related to members of this family, which we have termed Pdk1p. Pdk1p localizes to the spindle pole body and the actomyosin ring in early mitotic cells. Cells deleted for pdk1 display multiple defects in mitosis and cytokinesis, all of which are exacerbated when the function of fission yeast polo kinase, Plo1p, is partially compromised. We conclude that Pdk1p functions in concert with Plo1p to regulate multiple processes such as the establishment of a bipolar mitotic spindle, transition to anaphase, placement of the actomyosin ring and proper execution of cytokinesis. We also present evidence that the effects of Pdk1p on cytokinesis are likely mediated via the fission yeast anillin-related protein, Mid1p and the septation initiation network (SIN).

Address correspondence to: Mohan K. Balasubramanian (mohan{at}tll.org.sg)




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