Interrogating signaling nodes involved in cellular transformations using kinase activity probes

Cliff I. Stains, Nathan C. Tedford, Traci C. Walkup, Elvedin Luković, Brenda N. Goguen, Linda G. Griffith, Douglas A. Lauffenburger, Barbara Imperiali

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)210-217
Number of pages8
JournalChemistry and Biology
Issue number2
StatePublished - Feb 24 2012
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry


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