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The role of endoplasmic reticulum‐associated protein degradation in MHC class I antigen processing
Author(s) -
Wang Ye,
Chen Di,
Androlewicz Matthew J.
Publication year - 1999
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/j.1600-065x.1999.tb01356.x
Subject(s) - antigen processing , endoplasmic reticulum associated protein degradation , endoplasmic reticulum , transporter associated with antigen processing , mhc class i , antigen presentation , microbiology and biotechnology , biology , antigen , glycoprotein , major histocompatibility complex , cytosol , protein degradation , unfolded protein response , biochemistry , immunology , immune system , t cell , enzyme
Summary: The processing and presentation of secretory glycoprotein antigens by the MHC class I processing pathway presents an interesting topological problem. That is, how do the luminal glycoprotein antigens gain access to the class I processing machinery located in the cell cytosol? Current data indicate that the retrograde transport of glycoproteins from the endoplasmic reticulum (ER) to cytosol represents the major pathway for ER‐associated protein degradation, and most likely represents a major pathway for the processing of glycoprotein antigens by MHC class I molecules as well. There is now a growing list of viral and tumor glycoprotein antigens that undergo retrograde transport from the ER to the cytosol and processing by the ubiquitin‐proteasome pathway of degradation. We review here some general aspects of this “ER degradation” pathway, and how it relates to the processing and presentation of class I‐associated viral and tumor antigens. In particular, we analyze the role of oligosaccharide trimming and ER molecular chaperones in this process. We would like to emphasize that the class I processing machinery has adapted a common cellular pathway for its use, and that this could lead to the identification of unique characteristics with regard to ER degradation and antigen processing.