In vivo control of endosomal architecture by class II-associated invariant chain and cathepsin S

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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.
Publisher
WILEY-V C H VERLAG GMBH
Issue Date
2005-09
Language
English
Article Type
Article
Keywords

MHC CLASS-II; ANTIGEN PRESENTATION; DENDRITIC CELLS; CYTOPLASMIC TAIL; MICE LACKING; ENDOCYTIC COMPARTMENTS; MOLECULES; TRANSPORT; COMPLEX; DEGRADATION

Citation

EUROPEAN JOURNAL OF IMMUNOLOGY, v.35, no.9, pp.2552 - 2562

ISSN
0014-2980
DOI
10.1002/eji.200526323
URI
http://hdl.handle.net/10203/240863
Appears in Collection
MSE-Journal Papers(저널논문)
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