Visualization of Protein-Specific Glycosylation inside Living Cells

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Protein glycosylation is a ubiquitous post-translational modification that is involved in the regulation of many aspects of protein function. In order to uncover the biological roles of this modification, imaging the glycosylation state of specific proteins within living cells would be of fundamental importance. To date, however, this has not been achieved. Herein, we demonstrate protein-specific detection of the glycosylation of the intracellular proteins OGT, Foxo1, p53, and Akt1 in living cells. Our generally applicable approach relies on Diels-Alder chemistry to fluorescently label intracellular carbohydrates through metabolic engineering. The target proteins are tagged with enhanced green fluorescent protein (EGFP). Förster resonance energy transfer (FRET) between the EGFP and the glycan-anchored fluorophore is detected with high contrast even in presence of a large excess of acceptor fluorophores by fluorescence lifetime imaging microscopy (FLIM).

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ISO 690DOLL, Franziska, Annette BUNTZ, Anne-Katrin SPÄTE, Verena F. SCHART, Alexander TIMPER, Waldemar SCHRIMPF, Christof R. HAUCK, Andreas ZUMBUSCH, Valentin WITTMANN, 2016. Visualization of Protein-Specific Glycosylation inside Living Cells. In: Angewandte Chemie International Edition. 2016, 55(6), pp. 2262-2266. ISSN 0570-0833. eISSN 1521-3773. Available under: doi: 10.1002/anie.201503183
BibTex
@article{Doll2016Visua-33637,
  year={2016},
  doi={10.1002/anie.201503183},
  title={Visualization of Protein-Specific Glycosylation inside Living Cells},
  number={6},
  volume={55},
  issn={0570-0833},
  journal={Angewandte Chemie International Edition},
  pages={2262--2266},
  author={Doll, Franziska and Buntz, Annette and Späte, Anne-Katrin and Schart, Verena F. and Timper, Alexander and Schrimpf, Waldemar and Hauck, Christof R. and Zumbusch, Andreas and Wittmann, Valentin}
}
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