The cell biology of major histocompatibility complex class I assembly: towards a molecular understanding
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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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.
|Digital Object Identifier (DOI):||doi:10.1111/j.1399-0039.2010.01550.x|
|Keywords:||major histocompatibility complex, antigen presentation, peptide selection, peptide loading complex, tapasin, eraap, calreticulin, immunodominance|
|Subjects:||Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH426 Genetics
Q Science > QR Microbiology > QR180 Immunology
|Date Deposited:||30 Nov 2010 15:08|
|Last Modified:||20 Feb 2017 09:42|
Funded by: CRUK (UNSPECIFIED)
UNSPECIFIED to UNSPECIFIED
|Further Information:||Google Scholar|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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