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Active kinase proteome screening reveals novel signal complexity in cardiomyopathy.

Authors: Fernando, P  Deng, W  Pekalska, B  DeRepentigny, Y  Kothary, R  Kelly, JF  Megeney, LA 
Citation: Fernando P, etal., Mol Cell Proteomics. 2005 May;4(5):673-82. Epub 2005 Feb 18.
Pubmed: (View Article at PubMed) PMID:15722372
DOI: Full-text: DOI:10.1074/mcp.M400200-MCP200

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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CRRD Object Information
CRRD ID: 1582275
Created: 2006-11-03
Species: All species
Last Modified: 2006-11-03
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.