Tapasin: an ER chaperone that controls MHC class I assembly with peptide |
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Authors: | Grandea A G Van Kaer L |
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Institution: | Howard Hughes Medical Institute, Dept of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232-0295, USA. |
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Abstract: | The stable assembly of MHC class I molecules with peptides in the endoplasmic reticulum (ER) involves several accessory molecules. One of these accessory molecules is tapasin, a transmembrane protein that tethers empty class I molecules to the peptide transporter associated with antigen processing (TAP). Here, evidence is presented that tapasin retains class I molecules in the ER until they acquire high-affinity peptides. |
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