Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP.

@article{Sadasivan1996RolesFC,
  title={Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP.},
  author={Bhanu K. Sadasivan and Paul J Lehner and Bodo Ortmann and Thomas Spies and Peter Cresswell},
  journal={Immunity},
  year={1996},
  volume={5 2},
  pages={
          103-14
        }
}
Assembly of MHC class I-beta 2 microglobulin (beta 2m) dimers in the endoplasmic reticulum involves two chaperones. Calnexin has previously been shown to interact with free class I heavy chains. Here, we show that the related chaperone, calreticulin, binds human class I-beta 2m dimers prior to peptide loading. Calreticulin remains associated with at least a subset of class I molecules when they, in turn, bind to TAP. Further evidence suggests that the interaction of class I-beta 2m dimers with… CONTINUE READING
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