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A Cell‐Permeable ATP Analogue for Kinase‐Catalyzed Biotinylation
Author(s) -
Fouda Ahmed E.,
Pflum Mary Kay H.
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201503041
Subject(s) - biotinylation , biochemistry , kinase , phosphoprotein , chemistry , cell , phosphorylation , lysis , protein kinase a , enzyme , microbiology and biotechnology , biology
ATP analogues have been powerful compounds for the study of kinase‐catalyzed phosphorylation. However, the cell impermeability of ATP analogues has largely limited their use to in vitro lysate‐based experiments. Herein, we report the first cell‐permeable ATP analogue, ATP–polyamine–biotin (APB). APB is shown to promote biotin labeling of kinase substrates in live cells and has future applications in phosphoprotein purification and analysis. More generally, these studies provide a foundation for the development of additional cell‐permeable ATP analogues for cell‐signaling research.