Interrogating Signaling Nodes Involved in Cellular Transformations Using Kinase Activity Probes
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Stains-2012-Interrogating Signal.pdf
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Author(s)
Stains, Cliff I.
Tedford, Nathan C.
Walkup, Traci C.
Lukovic, Elvedin
Goguen, Brenda N.
Griffith, Linda G.
Lauffenburger, Douglas A.
Imperiali, Barbara
Date Issued
February 2012
Journal
Chemistry and Biology
Publisher
Elsevier
Citation
Stains, Cliff I., Nathan C. Tedford, Traci C. Walkup, Elvedin Lukovic, Brenda N. Goguen, Linda G. Griffith, Douglas A. Lauffenburger, and Barbara Imperiali. “Interrogating Signaling Nodes Involved in Cellular Transformations Using Kinase Activity Probes.” Chemistry & Biology 19, no. 2 (February 2012): 210–217. © 2012 Elsevier Ltd.
Version
Final published version
Abstract
Protein kinases catalyze protein phosphorylation and thereby control the flow of information through signaling cascades. Currently available methods for concomitant assessment of the enzymatic activities of multiple kinases in complex biological samples rely on indirect proxies for enzymatic activity, such as posttranslational modifications to protein kinases. Our laboratories have recently described a method for directly quantifying the enzymatic activity of kinases in unfractionated cell lysates using substrates containing a phosphorylation-sensitive unnatural amino acid termed CSox, which can be monitored using fluorescence. Here, we demonstrate the utility of this method using a probe set encompassing p38α, MK2, ERK1/2, Akt, and PKA. This panel of chemosensors provides activity measurements of individual kinases in a model of skeletal muscle differentiation and can be readily used to generate individualized kinase activity profiles for tissue samples from clinical cancer patients.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
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Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
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DOI of Published Version
https://doi.org/10.1016/j.chembiol.2011.11.012
