Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity.

ABSTRACT: Protein sulfenylation is a post-translational modification of emerging importance in higher eukaryotes. However, investigation of its diverse roles remains challenging, particularly within a native cellular environment. Herein we report the development and application of DYn-2, a new chemoselective probe for detecting sulfenylated proteins in human cells. These studies show that epidermal growth factor receptor-mediated signaling results in H(2)O(2) production and oxidation of downstream proteins. In addition, we demonstrate that DYn-2 has the ability to detect differences in sulfenylation rates within the cell, which are associated with differences in target protein localization. We also show that the direct modification of epidermal growth factor receptor by H(2)O(2) at a critical active

SUBMITTER: Paulsen CE 

PROVIDER: S-EPMC3528018 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature