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A Cell-Permeable ATP Analogue for Kinase-Catalyzed Biotinylation.

ABSTRACT: 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.

SUBMITTER: Fouda AE

PROVIDER: S-EPMC4551444 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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A Cell-Permeable ATP Analogue for Kinase-Catalyzed Biotinylation.

Fouda Ahmed E AE Pflum Mary Kay H MK

Angewandte Chemie (International ed. in English) 20150626 33

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 ...[more]

PMID: 26119262

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