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Volume 270, Number 36, Issue of September 08, pp. 21086-21091, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Polo-like Kinase Is a Cell Cycle-regulated Kinase Activated during Mitosis

(Received for publication, April 5, 1995; and in revised form, June 12, 1995)

Ryoji Hamanaka ,&nbsp;<WBR> Mark R. Smith ,&nbsp;<WBR> Patrick M. O'Connor ,&nbsp;<WBR> Sharon Maloid ,&nbsp;<WBR> Kelly Mihalic ,&nbsp;<WBR> Jerry L. Spivak ,&nbsp;<WBR> Dan L. Longo ,&nbsp;<WBR> Douglas K. Ferris

Previously, we demonstrated that expression of polo-like kinase (PLK) is required for cellular DNA synthesis and that overexpression of PLK is sufficient to induce DNA synthesis. We now report that the endogenous levels of PLK, its phosphorylation status, and protein kinase activity are tightly regulated during cell cycle progression. PLK protein is low in G(1), accumulates during S and G(2)M, and is rapidly reduced after mitosis. During mitosis, PLK is phosphorylated on serine, and its serine threonine kinase function is activated at a time close to that of p34. The phosphorylated form of PLK migrates with reduced mobility on SDS-polyacrylamide gel electrophoresis, and dephosphorylation by purified protein phosphatase 2A converts it to the more rapidly migrating form and reduces the total amount of PLK kinase activity. Purified p34-cyclin B complex can phosphorylate PLK protein in vitro but causes little increase in PLK kinase activity.



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