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(The FASEB Journal. 2004;18:31-38.)
© 2004 FASEB

Quality control of MHC class I maturation

KAJSA M. PAULSSON*,{dagger},1 and PING WANG{dagger}

* Rayne institute, Centre for Molecular medicine, Department of Medicine, University College of London, London WC1E 6JJ, UK; and
{dagger} Immunology Group, Institute of Cell and Molecular Science, Barts and The London School of Medicine and Dentistry, London, EC1A 7ED, UK

1Correspondence: Rayne Institute, Centre for Molecular Medicine, Department of Medicine, University College of London, 5 University St., London WC1E 6JJ, UK. E-mail: k.paulsson{at}ucl.ac.uk

Assembly of MHC class I molecules in the ER is regulated by the so-called loading complex (LC). This multiprotein complex is of definite importance for class I maturation, but its exact organization and order of assembly are not known. Evidence implies that the quality of peptides loaded onto class I molecules is controlled at multiple stages during MHC class I assembly. We recently found that tapasin, an important component of the LC, interacts with COPI-coated vesicles. Biochemical studies suggested that the tapa-sin–COPI interaction regulates the retrograde transport of immature MHC class I molecules from the Golgi network back to the ER. Also other findings now propose that in addition to the peptide-loading control, the quality control of MHC class I antigen presentation includes the restriction of export of suboptimally loaded MHC class I molecules to the cell surface. In this review, we use recent studies of tapasin to examine the efficiency of TAP, the LC constitution, ER quality control of class I assembly, and peptide optimization. The concepts of MHC class I recycling and ER retention are also discussed.—Paulsson, K. M., Wang, P. Quality control of MHC class I maturation.


Key Words: loading complex • tapasin • TAP • peptide • COPI • transport • optimization




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