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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

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IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

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1437-4315
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Volume 385, Issue 9 (Sep 2004)

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Tapasin and other chaperones: models of the MHC class I loading complex

Cynthia Anne Wright / Patrycja Kozik / Martin Zacharias
  • Bioinformatics and Computational Biology, International University Bremen, D-28759 Bremen, Germany
  • Other articles by this author:
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/ Sebastian Springer
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2004.100

Abstract

MHC (major histocompatibility complex) class I molecules bind intracellular virus-derived peptides in the endoplasmic reticulum (ER) and present them at the cell surface to cytotoxic T lymphocytes. Peptide-free class I molecules at the cell surface, however, could lead to aberrant T cell killing. Therefore, cells ensure that class I molecules bind high-affinity ligand peptides in the ER, and restrict the export of empty class I molecules to the Golgi apparatus. For both of these safeguard mechanisms, the MHC class I loading complex (which consists of the peptide transporter TAP, the chaperones tapasin and calreticulin, and the protein disulfide isomerase ERp57) plays a central role. This article reviews the actions of accessory proteins in the biogenesis of class I molecules, specifically the functions of the loading complex in high-affinity peptide binding and localization of class I molecules, and the known connections between these two regulatory mechanisms. It introduces new models for the mode of action of tapasin, the role of the class I loading complex in peptide editing, and the intracellular localization of class I molecules.

Keywords: calreticulin; ERp57; major histocompatibility complex molecules; peptide binding; TAP; tapasin

References

About the article

Published Online: 2005-06-01

Published in Print: 2004-09-01


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2004.100.

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