scholarly journals 4-Deoxy-4-fluoro-GalNAz (4FGalNAz) Is a Metabolic Chemical Reporter of O-GlcNAc Modifications, Highlighting the Notable Substrate Flexibility of O-GlcNAc Transferase

2021 ◽  
Author(s):  
Emma G. Jackson ◽  
Giuliano Cutolo ◽  
Bo Yang ◽  
Nageswari Yarravarapu ◽  
Mary W. N. Burns ◽  
...  
Keyword(s):  
Chemical Reporter ◽  
Glcnac Transferase

scholarly journals Exploring the Potential of β-Catenin O-GlcNAcylation by Using Fluorescence-Based Engineering and Imaging

Molecules ◽  
2020 ◽  
Vol 25 (19) ◽  
pp. 4501
Author(s):  
Angelina Kasprowicz ◽  
Corentin Spriet ◽  
Christine Terryn ◽  
Vincent Rigolot ◽  
Stephan Hardiville ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Sequence ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Large Family ◽  
Post Translational Modifications ◽  
Chemical Reporter ◽  
Green Fluorescent ◽  
Glcnac Transferase

Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs). We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells. We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay. We validated this technology by imaging the O-GlcNAcylation status of β-catenin in HeLa cells. The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). Finally, we provided a flowchart demonstrating how this technology is transposable to any kind of glycosylation.

scholarly journals Exploring the Potential of β-Catenin O-GlcNAcylation by Using Fluorescence-Based Engineering and Imaging

2020 ◽  
Author(s):  
Angelina Kasprowicz ◽  
Corentin Spriet ◽  
Christine Terryn ◽  
Matthew G. Alteen ◽  
Tony Lefebvre ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Sequence ◽  
Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Large Family ◽  
Post Translational Modifications ◽  
Chemical Reporter ◽  
Green Fluorescent ◽  
Glcnac Transferase

Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs). We have developed an original tool enabling labeling and visualization of the cell cycle key-regulator b-catenin in its O-GlcNAcylated form based on intramolecular Förster resonance energy transfer (FRET) technology in cells. We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of b-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM resulting in a fast and easy to monitor qualitative FRET assay. We validated this technology by imaging the O-GlcNAcylation status of b-catenin in HeLa cells. Moreover, the changes in O-GlcNAcylation of b-catenin were varied by perturbing global cellular O-GlcNAc levels with inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). Finally, we provided a flowchart demonstrating how this technology is transposable to any kind of glycosylation.

216-OR: O-GlcNAc Transferase in the Ventromedial Hypothalamus Regulates Lipid Metabolism through Fat Depot–Specific Sympathetic Innervation

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 216-OR
Author(s):  
QI WANG ◽  
BICHEN ZHANG ◽  
YUNFAN YANG ◽  
JIA MI ◽  
GENG TIAN ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Sympathetic Innervation ◽  
Ventromedial Hypothalamus ◽  
Fat Depot ◽  
Glcnac Transferase

scholarly journals O-linked N-acetylglucosamine transferase is involved in fine regulation of flowering time in winter wheat

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Min Fan ◽  
Fang Miao ◽  
Haiyan Jia ◽  
Genqiao Li ◽  
Carol Powers ◽  
...  
Keyword(s):  
Winter Wheat ◽  
Flowering Time ◽  
Heading Date ◽  
Wheat Cultivars ◽  
Gene Encoding ◽  
Constitutive Overexpression ◽  
Winter Wheat Cultivars ◽  
Fine Regulation ◽  
Trait Locus ◽  
Glcnac Transferase

AbstractVernalization genes underlying dramatic differences in flowering time between spring wheat and winter wheat have been studied extensively, but little is known about genes that regulate subtler differences in flowering time among winter wheat cultivars, which account for approximately 75% of wheat grown worldwide. Here, we identify a gene encoding anO-linkedN-acetylglucosamine (O-GlcNAc) transferase (OGT) that differentiates heading date between winter wheat cultivars Duster and Billings. We clone thisTaOGT1gene from a quantitative trait locus (QTL) for heading date in a mapping population derived from these two bread wheat cultivars and analyzed in various environments. Transgenic complementation analysis shows that constitutive overexpression ofTaOGT1bfrom Billings accelerates the heading of transgenic Duster plants.TaOGT1 is able to transfer anO-GlcNAc group to wheat proteinTaGRP2. Our findings establish important roles forTaOGT1in winter wheat in adaptation to global warming in the future climate scenarios.

scholarly journals Regulating the Regulators: Mechanisms of Substrate Selection of the O-GlcNAc Cycling Enzymes OGT and OGA

Glycobiology ◽  
2021 ◽  
Author(s):  
Hannah M Stephen ◽  
Trevor M Adams ◽  
Lance Wells
Keyword(s):  
Nutrient Sensing ◽  
Substrate Selection ◽  
Disease States ◽  
Dynamic Modification ◽  
Selection For ◽  
Outstanding Question ◽  
Glcnac Transferase ◽  
Future Work ◽  
Partner Proteins ◽  
Selection Of

Abstract Thousands of nuclear and cytosolic proteins are modified with a single β-N-acetylglucosamine on serine and threonine residues in mammals, a modification termed O-GlcNAc. This modification is essential for normal development and plays important roles in virtually all intracellular processes. Additionally, O-GlcNAc is involved in many disease states, including cancer, diabetes, and X-linked intellectual disability. Given the myriad of functions of the O-GlcNAc modification, it is therefore somewhat surprising that O-GlcNAc cycling is mediated by only two enzymes: the O-GlcNAc transferase (OGT), which adds O-GlcNAc, and the O-GlcNAcase (OGA), which removes it. A significant outstanding question in the O-GlcNAc field is how do only two enzymes mediate such an abundant and dynamic modification. In this review, we explore the current understanding of mechanisms for substrate selection for the O-GlcNAc cycling enzymes. These mechanisms include direct substrate interaction with specific domains of OGT or OGA, selection of interactors via partner proteins, posttranslational modification of OGT or OGA, nutrient sensing, and localization alteration. Altogether, current research paints a picture of an exquisitely regulated and complex system by which OGT and OGA select substrates. We also make recommendations for future work, toward the goal of identifying interaction mechanisms for specific substrates that may be able to be exploited for various research and medical treatment goals.

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