Related Experiment Video
Updated: May 20, 2026

Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
Published on: September 10, 2020
Structure, mechanism and inhibition of Golgi α-mannosidase II
1Department of Biology, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada. david.rose@uwaterloo.ca
Abstract:
The mature N-glycan on human glycoproteins is built up by the activity and regulation of enzymes in the endoplasmic reticulum and Golgi apparatus. A key enzyme in the maturation of N-glycans is the first glycoside hydrolase in the Golgi pathway, α-mannosidase II (GMII). This enzyme has the unusual ability to cleave two different glycosidic linkages in it catalytic center. As such, it removes two terminal mannoses following the activity of N-acetyl-glucosaminyl transferase I, and is a critical step in the formation of mature glycans. Structural analyses of the Drosophila homologue of GMII have led to insights into its unusual mechanism and substrate specificity. In addition, the results build the foundation for the development of specific clinically relevant inhibitors.
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Golgi Matrix Proteins
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
Transport Across the Golgi
Enzyme Inhibition
ATP Synthase: Mechanism
Export of Misfolded Proteins out of the ER

