Chaperones and folding of MHC class I molecules in the endoplasmic reticulum |
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Authors: | Paulsson Kajsa Wang Ping |
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Institution: | The Institution of Tumour Immunology, Lund University, BMC I12, S-223 62, Lund, Sweden. kajsa.paulsson@wblab.lu.se |
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Abstract: | In this review we discuss the influence of chaperones on the general phenomena of folding as well as on the specific folding of an individual protein, MHC class I. MHC class I maturation is a highly sophisticated process in which the folding machinery of the endoplasmic reticulum (ER) is heavily involved. Understanding the MHC class I maturation per se is important since peptides loaded onto MHC class I molecules are the base for antigen presentation generating immune responses against virus, intracellular bacteria as well as tumours. This review discusses the early stages of MHC class I maturation regarding BiP and calnexin association, and differences in MHC class I heavy chain (HC) interaction with calnexin and calreticulin are highlighted. Late stage MHC class I maturation with focus on the dedicated chaperone tapasin is also discussed. |
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