التفاصيل البيبلوغرافية
| العنوان: |
Next‐Generation Metabolic Glycosylation Reporters Enable Detection of Protein O−GlcNAcylation in Living Cells without S‐Glyco Modification. |
| المؤلفون: |
Kufleitner, Markus, Haiber, Lisa Maria, Li, Shuang, Surendran, Harsha, Mayer, Thomas U., Zumbusch, Andreas, Wittmann, Valentin |
| المصدر: |
Angewandte Chemie International Edition; 5/13/2024, Vol. 63 Issue 20, p1-9, 9p |
| مصطلحات موضوعية: |
POST-translational modification, FLUORESCENCE resonance energy transfer, DIELS-Alder reaction, NUCLEAR proteins, GLYCOSYLATION |
| مستخلص: |
Protein O−GlcNAcylation is a ubiquitous posttranslational modification of cytosolic and nuclear proteins involved in numerous fundamental regulation processes. Investigation of O−GlcNAcylation by metabolic glycoengineering (MGE) has been carried out for two decades with peracetylated N‐acetylglucosamine (GlcNAc) and N‐acetylgalactosamine derivatives modified with varying reporter groups. Recently, it has been shown that these derivatives can result in non‐specific protein labeling termed S‐glyco modification. Here, we report norbornene‐modified GlcNAc derivatives with a protected phosphate at the anomeric position and their application in MGE. These derivatives overcome two limitations of previously used O−GlcNAc reporters. They do not lead to detectable S‐glyco modification, and they efficiently react in the inverse‐electron‐demand Diels–Alder (IEDDA) reaction, which can be carried out even within living cells. Using a derivative with an S‐acetyl‐2‐thioethyl‐protected phosphate, we demonstrate the protein‐specific detection of O−GlcNAcylation of several proteins and the protein‐specific imaging of O−GlcNAcylation inside living cells by Förster resonance energy transfer (FRET) visualized by confocal fluorescence lifetime imaging microscopy (FLIM). [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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