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Related Concept Videos

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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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,...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.

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Updated: Jun 11, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell

Lavinia Bhatt1, Claire Murphy, Liam S O'Driscoll

  • 1Department of Biochemistry, Biosciences Institute, University College Cork, Ireland.

The FEBS Journal
|July 13, 2010
PubMed
Summary
This summary is machine-generated.

Glycosylation is crucial for normal HFE protein function and cellular iron regulation. This study found that altering HFE glycosylation sites disrupts its trafficking and iron-binding capabilities, similar to hereditary hemochromatosis mutations.

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Last Updated: Jun 11, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Genetics

Background:

  • HFE protein is essential for iron homeostasis, regulating transferrin receptor binding.
  • N-glycosylation is a key post-translational modification for protein transport and function.
  • The role of HFE glycosylation in its localization and activity remained uninvestigated.

Purpose of the Study:

  • To investigate the impact of N-glycosylation on HFE protein localization and function.
  • To identify critical N-glycosylation sites on the human HFE protein.

Main Methods:

  • Bioinformatic analysis to predict N-glycosylation sites.
  • Site-directed mutagenesis to create HFE mutants (single, double, triple).
  • Confocal microscopy to assess protein localization and co-localization studies.
  • Functional assays measuring beta2-microglobulin interaction and transferrin binding.

Main Results:

  • The HFE triple mutant, lacking glycosylation, mislocalized to the endoplasmic reticulum, similar to the HFE-C282Y mutant.
  • The triple mutant exhibited functional deficiencies in beta2-microglobulin interactions and transferrin binding regulation.
  • Single and double mutants showed mixed localization and impaired transferrin binding, indicating a dose-dependent effect of glycosylation.

Conclusions:

  • N-glycosylation is vital for the proper intracellular trafficking of HFE protein.
  • Glycosylation is essential for the functional activity of HFE in regulating cellular iron levels.
  • Disruption of HFE glycosylation mimics aspects of hereditary hemochromatosis.