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Related Concept Videos

Proteoglycans01:05

Proteoglycans

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,...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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.
Multiple sugar molecules that may or may...
Protein Glycosylation01:25

Protein Glycosylation

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.
Glycosylation occurs in...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

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Generation of Monocyte-Derived Dendritic Cells with Differing Sialylated Phenotypes
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Distinct O-Linked Glycosylation Systems in Signaling and Immune Regulation.

Shuguang Wang1, Shibo Xiao1, Yuman Huang1

  • 1Health Science Center, Yangtze University, Jingzhou 434023, China.

International Journal of Molecular Sciences
|June 12, 2026
PubMed
Summary

Two O-linked glycosylation systems, mucin-type O-GalNAc glycosylation and O-GlcNAcylation, regulate distinct cellular processes. Despite differences, both impact signaling, immune homeostasis, and disease susceptibility.

Keywords:
O-glycosylationcell signalingdisease pathogenesisglycoproteomicsimmune regulation

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Immunology

Background:

  • O-linked glycosylation involves distinct regulatory systems: mucin-type O-GalNAc glycosylation and intracellular O-GlcNAcylation.
  • Both target serine/threonine residues but differ in glycan structure, cellular compartment, enzymatic machinery, and biological function.

Purpose of the Study:

  • To review and summarize evidence on the distinct roles and convergence of mucin-type O-GalNAc glycosylation and O-GlcNAcylation.
  • To discuss the connection between glycosylation defects, genetic variation, and disease phenotypes.
  • To highlight recent advances and limitations in glycoproteomics for studying O-linked glycosylation.

Main Methods:

  • Targeted literature searches of PubMed, Web of Science, and related databases.
  • Keyword-based searches included O-glycosylation, O-GalNAc glycosylation, O-GlcNAcylation, immune regulation, cell signaling, glycoproteomics, and congenital disorders of glycosylation (CDG).
  • Review and synthesis of evidence from selected studies.

Main Results:

  • Mucin-type O-glycosylation regulates receptor behavior, cell adhesion, immune checkpoints, immunoglobulin function, antigen recognition, and pathogen-host interactions.
  • O-GlcNAcylation primarily modulates intracellular signaling, transcriptional control, stress responses, post-translational modification crosstalk, and innate immune pathways.
  • Glycosylation defects, including CDG, link genetic variation to disease phenotypes.

Conclusions:

  • Distinct O-linked glycosylation systems employ different molecular mechanisms but converge on regulating signaling, immune homeostasis, and disease susceptibility.
  • Advances in glycoproteomics offer improved mechanistic insights but face limitations in site localization, structural resolution, and functional validation.
  • Understanding these glycosylation pathways is crucial for deciphering disease mechanisms and developing therapeutic strategies.