Editors' ChoiceProtein Domains

Looking for Like-Minded Partners

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Science's STKE  25 Feb 2003:
Vol. 2003, Issue 171, pp. tw86-TW86
DOI: 10.1126/stke.2003.171.tw86

Protein kinases are regulators of many biological processes, but many of the targets of these phosphorylating enzymes remain unidentified. Some proteins have special binding domains that preferentially recognize phosphorylated amino acids, and both the kinases that modify these sites and the binding partners that recognize them look for similar sequence motifs. Elia et al. (see the Perspective by Silljé and Nigg) developed a proteomic screen to identify certain binding domains and used it to search for proteins involved in the control of cell division. The screen revealed a phosphoprotein-binding domain, the Polo-box domain (PBD), itself located in a protein kinase, Polo-like kinase 1 (Plk-1). Further experiments indicated that the PBD promotes subcellular localization of Plk1 and the interaction of Plk1 with its substrates in response to the action of mitotic kinases.

A. E. H. Elia, L. C. Cantley, M. B. Yaffe, Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 299, 1228-1231 (2003). [Abstract] [Full Text]

H. H. W. Silljé, E. A. Nigg, Capturing Polo kinase. Science 299, 1190-1191 (2003). [Summary] [Full Text]

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