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Reversible sulfenylation of the EGFR active siteAdd to my bookmarks

Nature Chemical Biology

December 12, 2011

A tool for the detection of a protein modification, called sulfenylation, in cells is reported this week in Nature Chemical Biology. EGFR, a receptor tyrosine kinase, activates growth-promoting pathways in response to extracellular signals; inappropriate activation of EGFR has been associated with multiple cancers. Activation of this kinase depends on a modification, called phosphorylation. Chemical modifications, in addition to phosphorylation, can also impact protein activity. One such modification, sulfenylation, has been challenging to monitor in cells. Kate Carroll and colleagues report a sensitive probe, called DYn-2, for detecting protein sulfenylation. They apply this probe to show that sulfenylation of EGFR enhances activity of this kinase. Because the site where this modification occurs is the target for potential cancer drugs that irreversibly inhibit EGFR, this discovery could have implications for the success of these drugs and for the interpretation of experiments employing these inhibitors as chemical probes.

DOI:10.1038/nchembio.736 | Original article

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