Related Experiment Video
Updated: Dec 2, 2025
11:21
Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
3.9K
Resolving the TorsinA Oligomerization Conundrum: The Glycan Hypothesis
Christian Fercher1, Lucía F Zacchi1
1Australian Research Council (ARC), Training Centre for Biopharmaceutical Innovation, The University of Queensland, St Lucia, QLD, Australia.
Frontiers in Molecular Biosciences
|November 2, 2020
Summary
TorsinA, a protein linked to Early Onset Torsion Dystonia, uses N-linked glycans to control its shape. These glycans promote an open structure, enabling torsinA to interact with cofactors for ATP hydrolysis.
Area of Science:
- Biochemistry
- Structural Biology
- Neuroscience
Background:
- TorsinA is a AAA+ ATPase implicated in Early Onset Torsion Dystonia.
- Its structural organization and function remain incompletely understood.
- Unlike other AAA+ ATPases, torsinA is a glycoprotein, with N-linked glycans influencing its biogenesis and localization.
Purpose of the Study:
- To investigate the role of torsinA's N-linked glycans in modulating its oligomerization properties.
- To explore how glycosylation affects torsinA's structural conformation and cofactor interactions.
Main Methods:
- Utilized structural modeling techniques.
- Analyzed the impact of N-linked glycans on torsinA's hexameric assembly.
Main Results:
- N-linked glycans appear to restrict the formation of closed homohexameric rings of torsinA.
- Glycans promote an open hexameric conformation.
- This open conformation facilitates interaction with essential cofactors for ATP hydrolysis.
Conclusions:
- TorsinA's N-linked glycans play a crucial role in regulating its oligomerization state.
- Glycosylation-induced conformational changes are key to torsinA's function in ATP hydrolysis.
- This represents a sophisticated example of molecular glycoengineering in nature.
Related Concept Videos
01:24Oligosaccharide Assembly
3.3K
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...
Multiple sugar molecules that may or may...
3.3K
01:05Proteoglycans
4.3K
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,...
4.3K
01:25Protein Glycosylation
8.6K
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...
Glycosylation occurs in...
8.6K
01:29Protein Folding Quality Check in the RER
4.8K
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...
4.8K