1. Interaction of the Thiol-Dependent Reductase ERp57 with Nascent Glycoproteins
- Author
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Neil J. Bulleid, Stephen High, Jason D. Oliver, and Fimme J. van der Wal
- Subjects
Glycosylation ,Saccharomyces cerevisiae Proteins ,Protein Disulfide-Isomerase Family ,Calnexin ,Biology ,Reductase ,Endoplasmic Reticulum ,Fungal Proteins ,chemistry.chemical_compound ,Dogs ,Microsomes ,Animals ,Enzyme Inhibitors ,Protein Precursors ,Isomerases ,Pancreas ,Heat-Shock Proteins ,Glycoproteins ,chemistry.chemical_classification ,Multidisciplinary ,Endoplasmic reticulum ,Calcium-Binding Proteins ,Indolizines ,Prolactin ,Molecular Weight ,Glucose ,Ribonucleoproteins ,chemistry ,Biochemistry ,Chaperone (protein) ,biology.protein ,Calreticulin ,Oxidoreductases ,Glycoprotein ,Glucosidases - Abstract
Calnexin and calreticulin interact specifically with newly synthesized glycoproteins in the endoplasmic reticulum (ER) and function as molecular chaperones. The carbohydrate-specific interactions between ER components and glycoproteins synthesized in isolated canine pancreatic microsomes were analyzed using a cross-linking approach. A carbohydrate-dependent interaction between newly synthesized glycoproteins, the thiol-dependent reductase ERp57, and either calnexin or calreticulin was identified. The interaction between ERp57 and the newly synthesized glycoproteins required trimming of the N-linked oligosaccharide side chain. Thus, it is likely that ERp57 functions as part of the glycoprotein-specific quality control machinery operating in the lumen of the ER.
- Published
- 1997
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