Current methods have limited ability in directly quantifying the extent of glutathionylation on specific protein-cysteines. In this issue of Cell Chemical Biology, Ahn et al. report G-ICAT (glutathione-based isotope-coded affinity tag), aimed at addressing this limitation. G-ICAT identifies Cysteine-692 within p120-catenin-a member of cadherin complex essential for cell-cell-contact maintenance-where C692-specific glutathionylation promotes E-cadherin destabilization.
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| http://dx.doi.org/10.1016/j.chembiol.2023.11.012 | DOI Listing |
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Tag, you're it: G-ICAT identifies p120-cysteine glutathionylation triggering E-cadherin destabilization.
Cell Chem Biol
December 2023
Swiss Federal Institute of Technology Lausanne, Lausanne, Switzerland. Electronic address:
Current methods have limited ability in directly quantifying the extent of glutathionylation on specific protein-cysteines. In this issue of Cell Chemical Biology, Ahn et al. report G-ICAT (glutathione-based isotope-coded affinity tag), aimed at addressing this limitation.
View Article and Find Full Text PDFChemoproteomic strategy identified p120-catenin glutathionylation regulates E-cadherin degradation and cell migration.
Cell Chem Biol
December 2023
Department of Chemistry, Drexel University, Philadelphia, PA 19104, USA. Electronic address:
Identification of cysteines with high oxidation susceptibility is important for understanding redox-mediated biological processes. In this report, we report a chemical proteomic strategy that finds cysteines with high susceptibility to S-glutathionylation. Our proteomic strategy, named clickable glutathione-based isotope-coded affinity tag (G-ICAT), identified 1,518 glutathionylated cysteines while determining their relative levels of glutathionylated and reduced forms upon adding hydrogen peroxide.
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