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Kinomics: methods for deciphering the kinome

Nature Methods volume 2, pages 17–25 (2005)Cite this article

Abstract

Phosphorylation by protein kinases is the most widespread and well-studied signaling mechanism in eukaryotic cells. Phosphorylation can regulate almost every property of a protein and is involved in all fundamental cellular processes. Cataloging and understanding protein phosphorylation is no easy task: many kinases may be expressed in a cell, and one-third of all intracellular proteins may be phosphorylated, representing as many as 20,000 distinct phosphoprotein states. Defining the kinase complement of the human genome, the kinome, has provided an excellent starting point for understanding the scale of the problem. The kinome consists of 518 kinases, and every active protein kinase phosphorylates a distinct set of substrates in a regulated manner. Deciphering the complex network of phosphorylation-based signaling is necessary for a thorough and therapeutically applicable understanding of the functioning of a cell in physiological and pathological states. We review contemporary techniques for identifying physiological substrates of the protein kinases and studying phosphorylation in living cells.

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Figure 1: Flow chart of strategies available for the identification of either substrate or kinase.

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Acknowledgements

We would like to acknowledge the critical reading and suggestions of S. Ghosh. T.H. is a Frank and Else Schilling American Cancer Society Research Professor. We apologize to workers in the field for omitting many relevant references and details due to lack of space.

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  1. Molecular and Cell Biology Laboratory, Salk Institute, 10010 North Torrey Pines Road, La Jolla, 92037, California, USA

    Sam A Johnson & Tony Hunter

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Correspondence to Tony Hunter.

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Johnson, S., Hunter, T. Kinomics: methods for deciphering the kinome. Nat Methods 2, 17–25 (2005). https://doi.org/10.1038/nmeth731

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