Visualizing specific protein glycoforms by transmembrane fluorescence resonance energy transfer

Yoshimi Haga, Kumiko Ishii, Kayo Hibino, Yasushi Sako, Yukishige Ito, Naoyuki Taniguchi and Tadashi Suzuki ()
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Yoshimi Haga: Glycometabolome Team, RIKEN Advanced Science Institute
Kumiko Ishii: Glycometabolome Team, RIKEN Advanced Science Institute
Kayo Hibino: Cellular Informatics Laboratory, RIKEN Advanced Science Institute
Yasushi Sako: Cellular Informatics Laboratory, RIKEN Advanced Science Institute
Yukishige Ito: Synthetic Cellular Chemistry Laboratory, RIKEN Advanced Science Institute
Naoyuki Taniguchi: Disease Glycomics Team, RIKEN Advanced Science Institute
Tadashi Suzuki: Glycometabolome Team, RIKEN Advanced Science Institute

Nature Communications, 2012, vol. 3, issue 1, 1-7

Abstract: Abstract Analyses of mice lacking glycosyltransferase have suggested that their pathological phenotypes are not attributable to the overall change of the sugar modification, but instead the result of changes of the glycan structures on a specific 'target' glycoprotein. Therefore, detecting or monitoring the glycosylation status of a specific protein in living cells is important, but no such methods are currently available. Here we demonstrate the detection of glycoforms of a specific glycoprotein using the fluorescence resonance energy transfer technique. Using model proteins, we detect characteristic fluorescence resonance energy transfer signals from the specific glycoform-bearing target glycoprotein. We also show that, upon insulin removal, sialylated glycoforms of green fluorescent protein-tagged GLUT4 seem to be internalized more slowly than non-sialylated GLUT4. This novel analytical imaging tool allows studying the roles of specific glycan modifications of a protein of interest.

Date: 2012
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DOI: 10.1038/ncomms1906

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