Related Experiment Video
Updated: Mar 31, 2026

4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Glycosylation-directed quality control of protein folding
Chengchao Xu1,2, Davis T W Ng1,2,3
1Temasek Life Sciences Laboratory, National University of Singapore, 1 Research Link, Singapore 117604.
Abstract:
Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated in the endoplasmic reticulum. These adducts have many biological functions, including, notably, their contribution to the maturation of glycoproteins. N-linked glycans are of oligomeric structure, forming configurations that provide blueprints to precisely instruct the folding of protein substrates and the quality control systems that scrutinize it. O-linked mannoses are simpler in structure and were recently found to have distinct functions in protein quality control that do not require the complex structure of N-linked glycans. Together, recent studies reveal the breadth and sophistication of the roles of these glycan-directed modifications in protein biogenesis.
Related Concept Videos
Protein Folding Quality Check in the RER
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Glycosylation
Glycosylation occurs in...
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

