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Method Article
Jean-Philippe Coppé
Kinome Activity Mapping
Corresponding Author
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Phosphorylation networks intimately regulate mechanisms of response to therapies. Identifying the phospho-catalytic activities of kinases in biological samples remains a challenge. Here, we introduce a high-throughput system to detect kinases’ enzymatic activity using their biological peptide targets as phospho-sensors. Libraries of peptides operate as specific, distinct combinatorial peptide sets that simultaneously distinguish and measure the activity of a multiplicity of kinase enzymes. Our strategy provides access to a vast, untapped resource of meaningful measurements, whether readouts are interpreted irrespective of which enzymes phosphorylate which probes, or analyzed to convert global phospho-signatures into functional profiles of kinase activities. The procedure described in this Protocol Exchange chapter focuses on detailing the statistical and computational analysis steps that allow deconvoluting peptide phosphorylation profiles into kinase activity signatures. This is related to the Nature Cell Biology manuscript NCB-C36710, titled: "Mapping phospho-catalytic dependencies of therapy-resistant tumors reveals actionable vulnerabilities".
Keywords
kinase enzymes, phospho-catalytic activity screening, peptide sensors, combinatorial profiling, cell extracts, tissue biospecimen extracts, functional proteomics, signaling networks
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Posted 12 Jun, 2019
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Subject Areas
Cell biology
Biological techniques
Mathematics and computing
Chemical biology
Computational biology and bioinformatics
Biochemistry
Associated Publications
Mapping phospho-catalytic dependencies of therapy-resistant tumours reveals actionable vulnerabilities
by Jean-Philippe Coppé, Miki Mori, Bo Pan, +17
Nature Cell Biology (03 June, 2019)
An open repository of community-contributed protocols sponsored by Nature Research.
Learn more about Protocol Exchange
Method Article
Jean-Philippe Coppé
Kinome Activity Mapping
Corresponding Author
Version History
CURRENT STATUS: Posted
Version 1
Posted 12 Jun, 2019
No community comments so far
Metrics
Comments: 0
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
Phosphorylation networks intimately regulate mechanisms of response to therapies. Identifying the phospho-catalytic activities of kinases in biological samples remains a challenge. Here, we introduce a high-throughput system to detect kinases’ enzymatic activity using their biological peptide targets as phospho-sensors. Libraries of peptides operate as specific, distinct combinatorial peptide sets that simultaneously distinguish and measure the activity of a multiplicity of kinase enzymes. Our strategy provides access to a vast, untapped resource of meaningful measurements, whether readouts are interpreted irrespective of which enzymes phosphorylate which probes, or analyzed to convert global phospho-signatures into functional profiles of kinase activities. The procedure described in this Protocol Exchange chapter focuses on detailing the statistical and computational analysis steps that allow deconvoluting peptide phosphorylation profiles into kinase activity signatures. This is related to the Nature Cell Biology manuscript NCB-C36710, titled: "Mapping phospho-catalytic dependencies of therapy-resistant tumors reveals actionable vulnerabilities".
none
Loading...
Associated Publications
Mapping phospho-catalytic dependencies of therapy-resistant tumours reveals actionable vulnerabilities
by Jean-Philippe Coppé, Miki Mori, Bo Pan, +17
Nature Cell Biology (03 June, 2019)