Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain

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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 beta(2)-microglobulin (beta(2)m) 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 beta(2)m to exit the ER, CD1d can be expressed on the cell surface as either a free heavy chain or associated with beta(2)m. 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.
Publisher
Amer Soc Biochemistry Molecular Biology Inc
Issue Date
2002-11
Language
English
Article Type
Article
Keywords

T-CELL RECOGNITION; CLASS-I MOLECULES; ENDOPLASMIC-RETICULUM; BIOCHEMICAL-CHARACTERIZATION; ALPHA-GALACTOSYLCERAMIDE; SURFACE EXPRESSION; SELF-GLYCOLIPIDS; LOADING COMPLEX; QUALITY-CONTROL; LYMPHOCYTES-T

Citation

JOURNAL OF BIOLOGICAL CHEMISTRY, v.277, no.47, pp.44838 - 44844

ISSN
0021-9258
DOI
10.1074/jbc.M207831200
URI
http://hdl.handle.net/10203/78741
Appears in Collection
BS-Journal Papers(저널논문)
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