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Related Concept Videos

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.
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...
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...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
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...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jul 20, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors
10:17

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Fucosylation in prokaryotes and eukaryotes.

Bing Ma1, Joanne L Simala-Grant, Diane E Taylor

  • 1Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.

Glycobiology
|September 16, 2006
PubMed
Summary

Fucosyltransferases (FucTs) are enzymes crucial for fucosylation in eukaryotes and prokaryotes. Comparing diverse FucTs reveals conserved mechanisms, offering potential for therapeutic glycoconjugate synthesis.

Area of Science:

  • Glycobiology
  • Enzymology
  • Molecular Biology

Background:

  • Fucosylation, the transfer of fucose, is vital in eukaryotic biological and pathological processes like development, inflammation, and metastasis.
  • While less common in prokaryotes, fucosylation plays roles in adhesion and immune modulation.
  • Fucosyltransferases (FucTs) catalyze fucose transfer, with mammalian FucTs serving as well-characterized models.

Purpose of the Study:

  • To review and highlight diverse FucT subfamilies across different organisms.
  • To explore the structural and mechanistic similarities between FucTs from various origins, particularly mammalian and prokaryotic.
  • To underscore the therapeutic potential of FucTs and their synthesized products.

Main Methods:

  • Comparative analysis of FucT domain structures and substrate specificities.

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

Published on: March 11, 2022

Related Experiment Videos

Last Updated: Jul 20, 2026

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors
10:17

Analysis of Fucosylated Human Milk Trisaccharides in Biotechnological Context Using Genetically Encoded Biosensors

Published on: April 13, 2019

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
12:29

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

Published on: March 11, 2022

  • Examination of sequence homology and functional similarities across FucT families.
  • Literature review of known FucT functions and applications.

    • Main Results:

    • Mammalian and Helicobacter pylori alpha1,3/4 FucTs exhibit functional similarity despite low sequence homology, suggesting conserved mechanisms.
    • Non-mammalian FucTs display varied domain structures and substrate specificities.
    • Unusual fucose linkages in plants and schistosomes indicate potential novel FucT subfamilies.

    Conclusions:

    • FucTs from different origins likely share conserved functional features and catalytic mechanisms.
    • Fucosyltransferases are valuable tools for synthesizing fucosylated compounds.
    • These synthesized glycoconjugates hold promise for treating infectious diseases, inflammatory conditions, and cancer metastasis.