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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

7.9K
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...
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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.
Multiple sugar molecules that may or may...
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Proteoglycans01:05

Proteoglycans

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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,...
4.1K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

4.3K
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...
4.3K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.9K
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...
5.9K
Glycosaminoglycans01:23

Glycosaminoglycans

5.5K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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Related Experiment Video

Updated: Oct 21, 2025

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

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N-Glycosylation.

Tetsuya Hirata1,2, Yasuhiko Kizuka3,4

  • 1Center for Highly Advanced Integration of Nano and Life Sciences (G-CHAIN), Gifu University, Gifu, Japan.

Advances in Experimental Medicine and Biology
|September 8, 2021
PubMed
Summary
This summary is machine-generated.

N-glycosylation is a crucial protein modification in humans, essential for protein folding and cellular functions. This process involves synthesizing N-glycan precursors in the ER and their maturation in the Golgi apparatus.

Keywords:
GlycosyltransferaseN-glycanOligosaccharyltransferase

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Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • N-glycosylation is a conserved modification affecting over 7000 human proteins.
  • It plays vital roles in protein folding, trafficking, and signal transduction, impacting physiological and pathological processes.

Purpose of the Study:

  • To provide an overview of the N-glycan biosynthetic pathway.
  • To detail N-glycan precursor synthesis in the endoplasmic reticulum (ER) and maturation in the Golgi apparatus.

Main Methods:

  • The chapter outlines the sequential enzymatic reactions involved in N-glycan precursor biosynthesis.
  • It describes the en bloc transfer of the oligosaccharide to nascent proteins.
  • Maturation processes involving glycosidases and glycosyltransferases in the Golgi are detailed.

Main Results:

  • The N-glycan precursor, Glc3Man9GlcNAc2, is synthesized in the ER.
  • N-glycans facilitate correct protein folding via chaperones like calnexin and calreticulin.
  • Misfolded glycoproteins are targeted for proteasomal degradation.
  • Further processing in the Golgi generates complex N-glycans, including branched structures.

Conclusions:

  • N-glycosylation is a complex, multi-step process critical for protein function and cellular health.
  • Understanding this pathway is essential for comprehending various physiological and pathological conditions.