Mannose 6-Phosphate Receptor Homology Domain-Containing Lectins in Mammalian Endoplasmic Reticulum-Associated Degradation
Mannose 6-Phosphate Receptor Homology Domain-Containing Lectins in Mammalian Endoplasmic Reticulum-Associated Degradation
Quality control of glycoproteins synthesized in the endoplasmic reticulum (ER) is mediated by lectins and molecular chaperones. N-linked Glc(3)Man(9)GlcNAc(2) oligosaccharides attached to the nascent polypeptides are processed and recognized by lectins in the ER. OS-9 and XTP3-B/Erlectin, mannose 6-phosphate receptor homology (MRH) domain-containing lectins in mammals, were recently identified as ER luminal glycoproteins that participate in ER-associated degradation (ERAD) of misfolded proteins. Frontal affinity chromatography (FAC) and cell-surface expressed lectin assay revealed that both OS-9 and XTP3-B recognize high-mannose type N-glycans that lack the terminal mannose on the C branch. Furthermore, these lectins associate with the HRD1-SEL1L ubiquitin ligase complex on the ER membrane. In this chapter, we describe the FAC methods used to analyze the carbohydrate-recognition specificity of OS-9 and methods to examine the interaction and the effect on ERAD of these proteins in vivo. We also discuss the structure and function of OS-9 and XTP3-B, and the effect of these lectins on ERAD.
- Nagoya City University Japan
- Kyoto University Japan
- Ochanomizu University Japan
- National Institutes of Natural Sciences Japan
Mammals, Sequence Homology, Amino Acid, Molecular Sequence Data, Endoplasmic Reticulum, Models, Biological, Chemistry Techniques, Analytical, Receptor, IGF Type 2, Protein Structure, Tertiary, Sequence Analysis, Protein, Lectins, Animals, Humans, Amino Acid Sequence, Protein Processing, Post-Translational, Phylogeny
Mammals, Sequence Homology, Amino Acid, Molecular Sequence Data, Endoplasmic Reticulum, Models, Biological, Chemistry Techniques, Analytical, Receptor, IGF Type 2, Protein Structure, Tertiary, Sequence Analysis, Protein, Lectins, Animals, Humans, Amino Acid Sequence, Protein Processing, Post-Translational, Phylogeny
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