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- W2018672094 abstract "The invariant chain (Ii) is a chaperone that regulates assembly and transport of class II MHC molecules. In the absence of the lysosomal protease cathepsin S (CatS), degradation of Ii is impaired and an Ii remnant that extends from the N terminus to about residue 110 accumulates in class II MHC-positive endosomal compartments, which are enlarged in size and lack multivesicular morphology. In primary B cells examined in vitro and in lymph nodes examined by immuno-electron microscopy, CatS controls architecture of class II-positive endosomal compartments. In a compound mutant mouse that lacks both CatS and Ii, the normal size of endosomes in class II-positive cells is restored, although internal endosomal membranes are absent. Proper degradation of Ii is thus essential for normal endosomal morphology in antigen-presenting cells in vivo." @default.
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- W2018672094 date "2005-09-01" @default.
- W2018672094 modified "2023-10-12" @default.
- W2018672094 title "In vivo control of endosomal architecture by class II-associated invariant chain and cathepsin S" @default.
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- W2018672094 doi "https://doi.org/10.1002/eji.200526323" @default.
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