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J. Biol. Chem., Vol. 277, Issue 47, 44838-44844, November 22, 2002
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From the Section of Immunobiology, Howard Hughes Medical Institute,
Yale University School of Medicine,
New Haven, Connecticut 06520-8011
Members of the CD1 family of membrane
glycoproteins can present antigenic lipids to T lymphocytes. Like major
histocompatibility complex class I molecules, they form a
heterodimeric complex of a heavy chain and
Calnexin, Calreticulin, and ERp57 Cooperate in Disulfide Bond
Formation in Human CD1d Heavy Chain*
2-microglobulin (2m) in the
endoplasmic reticulum (ER). Binding of lipid antigens, however, takes
place in endosomal compartments, similar to class II molecules, and on
the plasma membrane. Unlike major histocompatibility complex class I or
CD1b molecules, which need 2m to exit the ER, CD1d can
be expressed on the cell surface as either a free heavy chain or
associated with 2m. These differences led us to
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-butyldeoxynojirimycin. 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.
*
This work was supported by the Howard Hughes Medical
Institute and National Institutes of Health Grant AI23081.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 203-785-5176;
Fax: 203-737-1764; E-mail: peter.cresswell@yale.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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