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Molecular & Cellular Proteomics 4:673-682, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Active Kinase Proteome Screening Reveals Novel Signal Complexity in Cardiomyopathy^*

Pasan Fernando, Wen Deng, Beata Pekalska, Yves DeRepentigny, Rashmi Kothary^,¶, John F. Kelly and Lynn A. Megeney^,¶,||

From the Molecular Medicine Program, Ottawa Health Research Institute, Ottawa Hospital, Ottawa, Ontario K1H 8L6, Canada; Institute for Biologic Sciences, National Research Council, Ottawa, Ontario K1A 0R63, Canada; and ^¶ Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa K1H 8M5, Ontario, Canada

Recent advances in the characterization of the phosphoproteome have been limited to measuring phosphorylation statuses, which imply but do not measure protein kinase activity directly. As such, the ability to screen, compare, and define multiple protein enzymatic activities across divergent samples remains a daunting challenge in proteomics. Here, we describe a gel-based kinase assay coupled to MS identification as an approach to map global kinase activity and assign pathway architecture to specified biologic contexts. We demonstrate the utility of this method as a platform for the comparison of proteomes based on differences in both kinase activities and for use in the de novo substrate identification for individual kinases. This approach allowed us to map the signal perturbations in the post-natal heart that were associated with activation of a myopathic cascade as mediated by the mitogen-activated protein kinase MKK6 and established the novel observation that MKK6 promotes the development of cardiomyopathy through multiple substrate interactions.

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