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PMID:11825569
| Citation |
Gao, B, Adhikari, R, Howarth, M, Nakamura, K, Gold, MC, Hill, AB, Knee, R, Michalak, M and Elliott, T (2002) Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16:99-109 |
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| Abstract |
MHC class I molecules expressed in a calreticulin-deficient cell line (K42) assembled with beta 2-microglobulin (beta2-m) normally, but their subsequent loading with optimal peptides was defective. Suboptimally loaded class I molecules were released into the secretory pathway. This occurred despite the ability of newly synthesized class I to interact with the transporter associated with antigen processing (TAP) loading complex. The efficiency of peptide loading was reduced by 50%-80%, and impaired T cell recognition was observed for three out of four antigens tested. The peptide-loading function was specific to calreticulin, since the defect in K42 could be rectified by transfection with calreticulin but not a soluble form of calnexin, which shares its lectin-like activity. |
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| Keywords |
Animals; Antigen Presentation; Antiporters/chemistry; Biological Transport; Calcium-Binding Proteins/physiology; Calreticulin; Cells, Cultured; Endoplasmic Reticulum/metabolism; Heat-Shock Proteins/chemistry; Histocompatibility Antigens Class I/analysis; Histocompatibility Antigens Class I/chemistry; Histocompatibility Antigens Class I/physiology; Immunoglobulins/chemistry; Isomerases/chemistry; Membrane Transport Proteins; Mice; Protein Disulfide-Isomerases; Ribonucleoproteins/physiology |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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