title: 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.
authors.affiliation: Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48202 (USA) http://chem.wayne.edu/pflumgroup/
authors.forename: Ahmed E
authors.initials: AE
authors.lastname: Fouda
authors.affiliation: Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48202 (USA) http://chem.wayne.edu/pflumgroup/. pflum@chem.wayne.edu.
authors.forename: Mary Kay H
authors.initials: MK
authors.lastname: Pflum
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism*; D001710:Biotin / Q000031:analogs & derivatives* / Q000378:metabolism; D019921:Biotinylation / Q000379:methods; D002463:Cell Membrane Permeability; D006367:HeLa Cells; D006801:Humans; D062105:Molecular Docking Simulation; D011073:Polyamines / Q000737:chemistry* / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011073:Polyamines; D001710:Biotin; D000255:Adenosine Triphosphate; D011494:Protein Kinases
keywords: ATP; biotinylation; cell permeability; enzymes; kinases