The Thiol-dependent Reductase ERp57 Interacts Specifically with N-Glycosylated Integral Membrane Proteins

The lumen of the endoplasmic reticulum contains a number of distinct molecular chaperones and folding factors, which modulate the folding and assembly of newly synthesized proteins and protein complexes. A subset of these luminal components are specific for glycoproteins, and, like calnexin and calr...

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Bibliographic Details
Published in:The Journal of biological chemistry 1997-05, Vol.272 (21), p.13849-13855
Main Authors: Elliott, J G, Oliver, J D, High, S
Format: Article
Language:English
Subjects:
Animals
Autoantigens - metabolism
Calcium-Binding Proteins - metabolism
Calnexin
Calreticulin
Dogs
Endoplasmic Reticulum - enzymology
Glucose - metabolism
Glucose Transporter Type 1
Glycophorins - metabolism
Glycosylation
Heat-Shock Proteins - metabolism
Isomerases
Lectins - metabolism
Membrane Proteins - metabolism
Microsomes - metabolism
Molecular Chaperones - metabolism
Monosaccharide Transport Proteins - metabolism
Pancreas - cytology
Phosphoproteins - metabolism
Protein Binding
Protein Disulfide-Isomerases
Protein Folding
Rats
Ribonucleoproteins - metabolism
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Summary:The lumen of the endoplasmic reticulum contains a number of distinct molecular chaperones and folding factors, which modulate the folding and assembly of newly synthesized proteins and protein complexes. A subset of these luminal components are specific for glycoproteins, and, like calnexin and calreticulin, the thiol-dependent reductase ERp57 has been shown to interact specifically with soluble secretory proteins bearing N -linked carbohydrate. Calnexin and calreticulin also interact with glycosylated integral membrane proteins, and in this study we have examined the interaction of ERp57 with these substrates. As with soluble proteins, the binding of ERp57 to an integral membrane protein is dependent upon the protein bearing an N -glycan that has undergone glucose trimming. Furthermore, ERp57 binds to newly synthesized glycoproteins in combination with either calnexin or calreticulin. We propose that ERp57 acts in concert with calnexin and calreticulin to modulate glycoprotein folding and enforce the glycoprotein specific quality control mechanism operating in the endoplasmic reticulum.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.272.21.13849