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Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510
Heterodimers of MHC class I glycoprotein and
2-microglobulin (2m) bind short peptides
in the endoplasmic reticulum (ER). Before peptide binding these
molecules form part of a multisubunit loading complex that also
contains the two subunits of the TAP, the transmembrane glycoprotein
tapasin, the soluble chaperone calreticulin, and the thiol
oxidoreductase ERp57. We have investigated the assembly of the loading
complex and provide evidence that after TAP and tapasin associate with
each other, the transmembrane chaperone calnexin and ERp57 bind to the
TAP-tapasin complex to generate an intermediate. These interactions are
independent of the N-linked glycan of tapasin, but
require its transmembrane and/or cytoplasmic domain. This intermediate
complex binds MHC class I-2m dimers, an event
accompanied by the loss of calnexin and the acquisition of
calreticulin, generating the MHC class I loading complex. Peptide
binding then induces the dissociation of MHC class I-2m
dimers, which can be transported to the cell
surface.
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