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使用双功能小分子进行向蛋白O-GLNAcylation

Bowen Ma1, Khadija Shahed Khan1,2, Tongyang Xu1

  • 1School of Pharmacy, Faculty of Medicine, The Chinese University of Hong Kong, Sha Tin, Hong Kong.

Journal of the American Chemical Society
|April 1, 2024
PubMed
概括

研究人员开发了新的O-GlcNAcylation TArgeting Chimeras (OGTACs),以精确控制活细胞中的蛋白质O-GlcNAcylation. 这一突破使得在疾病和治疗开发中对O-GlcNAcylation进行有针对性的研究.

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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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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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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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