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Control of MHC class I traffic from the endoplasmic reticulum by cellular chaperones and viral anti-chaperones Gruhler A; Fruh KTraffic 2000[Apr]; 1 (4): 306-11MHC class I molecules assemble with peptides in the endoplasmic reticulum (ER). To ensure that only peptide-loaded MHC molecules leave the ER, empty molecules are retained by ER-resident chaperones, most notably the MHC-specific tapasin. ER exit of class I MHC is also controlled by viruses, but for the opposite purpose of preventing peptide presentation to T cells. Interestingly, some viral proteins are able to retain MHC class I molecules in the ER despite being transported. By contrast, other viral proteins exit the ER only upon binding to class I MHC, thereby rerouting newly synthesized class I molecules to intracellular sites of proteolysis. Thus, immune escape can be achieved by reversing, inhibiting or redirecting the chaperone-assisted MHC class I folding, assembly and intracellular transport.|*Molecular Chaperones[MESH]|Adenovirus Early Proteins/metabolism[MESH]|Animals[MESH]|Antiporters/metabolism[MESH]|Carrier Proteins/metabolism[MESH]|Endoplasmic Reticulum/*metabolism[MESH]|Glycoproteins/metabolism[MESH]|Golgi Apparatus/metabolism[MESH]|Histocompatibility Antigens Class I/*chemistry[MESH]|Humans[MESH]|Immediate-Early Proteins/metabolism[MESH]|Immunoglobulins/metabolism[MESH]|Membrane Glycoproteins/metabolism[MESH]|Membrane Proteins[MESH]|Membrane Transport Proteins[MESH]|Models, Biological[MESH]|Peptides/*metabolism[MESH]|Protein Transport[MESH]|RNA-Binding Proteins/metabolism[MESH]|Viral Envelope Proteins/metabolism[MESH]|Viral Proteins/metabolism[MESH]|Viruses/metabolism[MESH] |
