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The cell biology of major histocompatibility complex class I assembly: towards a molecular understanding

Record type: Article

Major histocompatibility complex class I (MHC I) proteins protect the host from intracellular pathogens and cellular abnormalities through the binding of peptide fragments derived primarily from intracellular proteins. These peptide-MHC complexes are displayed at the cell surface for inspection by cytotoxic T lymphocytes. Here we reveal how MHC I molecules achieve this feat in the face of numerous levels of quality control. Among these is the chaperone tapasin, which governs peptide selection in the endoplasmic reticulum as part of the peptide-loading complex, and we propose key amino acid interactions central to the peptide selection mechanism. We discuss how the aminopeptidase ERAAP fine-tunes the peptide repertoire available to assembling MHC I molecules, before focusing on the journey of MHC I molecules through the secretory pathway, where calreticulin provides additional regulation of MHC I expression. Lastly we discuss how these processes culminate to influence immune responses.

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Van Hateren, A., James, E., Bailey, A., Phillips, A., Dalchau, N. and Elliott, T. (2010) The cell biology of major histocompatibility complex class I assembly: towards a molecular understanding Tissue Antigens, 76, (4), pp. 259-75. (doi:10.1111/j.1399-0039.2010.01550.x). (PMID:21050182).

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Published date: October 2010
Keywords: major histocompatibility complex, antigen presentation, peptide selection, peptide loading complex, tapasin, eraap, calreticulin, immunodominance


Local EPrints ID: 168563
ISSN: 0001-2815
PURE UUID: 2ecda6b4-cfda-4b51-9779-0a99b202366f
ORCID for T. Elliott: ORCID iD

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Date deposited: 30 Nov 2010 15:08
Last modified: 18 Jul 2017 12:20

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Author: A. Van Hateren
Author: E. James
Author: A. Bailey
Author: A. Phillips
Author: N. Dalchau
Author: T. Elliott ORCID iD

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