ER quality control in the biogenesis of MHC class I molecules |
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| Authors: | Daniel C Chapman David B Williams |
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| Institution: | 1. Department of Immunology, University of Toronto, Toronto, Ontario, M5S 1A8, Canada;2. Department of Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada;1. UNIVERSITY OF READING;1. Department of Molecular Medicine, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia;2. Drug Design and Development Research Group, University of Malaya, 50603 Kuala Lumpur, Malaysia;1. Department of Internal Medicine IV, Saarland University, Homburg, Germany;2. Department of Transplant and Infection Immunology, Saarland University, Homburg, Germany;3. HLA-Laboratory, Stefan-Morsch-Stiftung, Birkenfeld, Germany;4. Department of Pathology, Saarland University, Homburg, Germany;1. National Resource for Automated Molecular Microscopy, The Department of Integrative Structural and Computational Biology, The Scripps Institute, La Jolla, CA 92037, United States;2. Division of Biomedical Informatics, University of California San Diego, 9500 Gilman Dr, La Jolla, CA 92093, United States;1. Department of Pathology, University of Massachusetts Medical School, Worcester, Massachusetts, USA;2. Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA |
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| Abstract: | Class I molecules of the major histocompatibility complex play a vital role in cellular immunity, reporting on the presence of viral or tumor-associated antigens by binding peptide fragments of these proteins and presenting them to cytotoxic T cells at the cell surface. The folding and assembly of class I molecules is assisted by molecular chaperones and folding catalysts that comprise the general ER quality control system which also monitors the integrity of the process, disposing of misfolded class I molecules through ER associated degradation (ERAD). Interwoven with general ER quality control are class I-specific components such as the peptide transporter TAP and the tapasin-ERp57 chaperone complex that supply peptides and monitor their loading onto class I molecules. This ensures that at the cell surface class I molecules will possess mainly optimal peptides with a long half-life. In this review we discuss these processes as well as a number of strategies that viruses have evolved to subvert normal class I assembly within the ER and thereby evade immune recognition by cytotoxic T cells. |
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