Lectins as chaperones in glycoprotein folding
Related Experiment Video
Updated: Oct 27, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
Published on: February 12, 2019
1Department of Cell Biology, Yale Medical School, New Haven, CT 06520-8002, USA. sergio.trombetta@yale.edu
Abstract:
N-glycosylation allows newly synthesized glycoproteins to interact with a lectin-based chaperone system in the endoplasmic reticulum. Binding to the lectins calnexin and calreticulin is mediated by monoglucosylated oligosaccharides that are produced transiently by the deglucosylation and reglucosylation of substrate glycoproteins during their maturation process. In mammalian cells, calnexin, calreticulin and associated factors promote the correct folding and oligomerization of many glycoproteins, providing unique quality control and chaperone functions specific for glycoproteins in the endoplasmic reticulum.
More Related Videos
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Protein Folding Quality Check in the RER
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding
Bacterial Protein Maturation

