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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Protein Glycosylation01:25

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Proteoglycans01:05

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules.

Bowen Ma1, Khadija Shahed Khan1,2, Tongyang Xu1

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|April 1, 2024
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Summary
This summary is machine-generated.

Researchers developed novel O-GlcNAcylation TArgeting Chimeras (OGTACs) to precisely control protein O-GlcNAcylation in living cells. This breakthrough enables targeted studies of O-GlcNAcylation in diseases and therapeutic development.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Protein O-linked β-N-acetylglucosamine modification (O-GlcNAcylation) is vital for cellular processes.
  • Dysregulated O-GlcNAcylation is implicated in diseases like cancer, diabetes, and neurodegeneration.
  • Existing chemical tools lack protein- and site-specificity for studying O-GlcNAcylation.

Purpose of the Study:

  • To develop novel chemical tools for precise control of protein O-GlcNAcylation.
  • To enable protein-specific O-GlcNAcylation in living cells.
  • To facilitate the study of O-GlcNAcylation's role in disease and therapeutic development.

Main Methods:

  • Development of heterobifunctional small molecules termed O-GlcNAcylation TArgeting Chimeras (OGTACs).
  • Utilizing OGTACs to recruit FKBP12F36V-fused O-GlcNAc transferase (OGT) to target proteins.
  • Demonstrating temporal, magnitude, and reversible control of O-GlcNAcylation in cellulo.

Main Results:

  • OGTACs successfully induced protein-specific O-GlcNAcylation of BRD4, CK2α, and EZH2 in living cells.
  • Achieved controllable O-GlcNAcylation with temporal, magnitude, and reversible characteristics.
  • Validated OGTACs as effective tools for modulating O-GlcNAcylation.

Conclusions:

  • OGTACs provide a powerful chemical platform for inducing protein-specific O-GlcNAcylation.
  • This technology enables detailed functional dissection of O-GlcNAcylation pathways.
  • OGTACs offer new therapeutic avenues for diseases linked to O-GlcNAcylation.