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- W1519291736 abstract "Th cells recognize peptide fragments of foreign Ags bound to MHC class II molecules. Upon synthesis in the endoplasmic reticulum, the alpha- and beta-chains of the class II molecules rapidly associate with invariant chains (li). The dissociation of li from class II molecules precedes binding of processed Ag and the formation of SDS-stable alpha beta dimers. We previously showed that functional, processed Ag-class II complexes are assembled in a dense lysosome-like compartment that contains stable class II molecules, but no li, referred to in this work as the peptide-loading compartment. We also identified a separate compartment that contains predominantly SDS-unstable li-class II complexes. Because we were unable to identify known organelle markers associated with this compartment, we refer to it as the X compartment. In this work, we provide results that indicate that the X compartment is composed of transport vesicles that move li-class II complexes to the peptide-loading compartment, where all events in the assembly of processed Ag-class II complexes occur." @default.
- W1519291736 created "2016-06-24" @default.
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- W1519291736 date "1995-09-15" @default.
- W1519291736 modified "2023-09-23" @default.
- W1519291736 title "Intracellular transport of invariant chain-MHC class II complexes to the peptide-loading compartment." @default.
- W1519291736 doi "https://doi.org/10.4049/jimmunol.155.6.2984" @default.
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