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Papers In Press, published online ahead of print September 17, 2002
Section of Immunobiology, Yale University School of Medicine, New Haven, CT 06520
Corresponding Author: peter.cresswell{at}yale.edu
Members of the CD1 family of membrane glycoproteins can present antigenic lipids to T lymphocytes. Like MHC class I molecules, they form a heterodimeric complex of a heavy chain and b2-microglobulin (b2m) in the ER. Binding of lipid antigens, however, takes place in endosomal compartments, similar to class II molecules, and on the plasma membrane. Unlike MHC class I or CD1b molecules, which need b2m to exit the ER, CD1d can be expressed on the cell surface as either a free heavy chain or associated with b2m. These differences led us investigate early events of CD1d biosynthesis and maturation and the role of ER chaperones in its assembly. Here we show that CD1d associates in the ER with both calnexin and calreticulin and with the thiol oxidoreductase ERp57 in a manner dependent on glucose trimming of its N-linked glycans. Complete disulfide bond formation in the CD1d heavy chain was substantially impaired if the chaperone interactions were blocked by the glucosidase inhibitors castanospermine or N-butyl-deoxynojirimycin. The formation of at least one of the disulfide bonds in the CD1d heavy chain is coupled to its glucose-trimming dependent association with ERp57, calnexin and calreticulin.
J. Biol. Chem, 10.1074/jbc.M207831200
Submitted on August 1, 2002
Revised on September 6, 2002
Accepted on September 17, 2002
Calnexin, calreticulin and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain
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