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Science 299 (5610): 1190-1191

Copyright © 2003 by the American Association for the Advancement of Science

SIGNAL TRANSDUCTION:
Capturing Polo Kinase

Herman H. W. Silljé and Erich A. Nigg

The interactions of kinases in signaling cascades and cell cycle pathways are so complex that it can be difficult to identify the protein binding domains that mediate these interactions. In a Perspective, Silljé and Nigg discuss a new proteomic screen (Elia et al.) that identifies the Polo-box binding domain of the mitotic kinase Plk1 as the domain that binds to phosphorylated sites in docking proteins such as Cdc25.


The authors are in the Department of Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany. E-mail: sillje{at}biochem.mpg.de, nigg@biochem.mpg.de


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Henipavirus V Protein Association with Polo-Like Kinase Reveals Functional Overlap with STAT1 Binding and Interferon Evasion.
L. E. Ludlow, M. K. Lo, J. J. Rodriguez, P. A. Rota, and C. M. Horvath (2008)
J. Virol. 82, 6259-6271
   Abstract »    Full Text »    PDF »
Distinct regulators for Plk1 activation in starfish meiotic and early embryonic cycles.
T. Okano-Uchida, E. Okumura, M. Iwashita, H. Yoshida, K. Tachibana, and T. Kishimoto (2003)
EMBO J. 22, 5633-5642
   Abstract »    Full Text »    PDF »

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