| First Author | Boes M | Year | 2005 |
| Journal | Eur J Immunol | Volume | 35 |
| Issue | 9 | Pages | 2552-62 |
| PubMed ID | 16094690 | Mgi Jnum | J:113490 |
| Mgi Id | MGI:3686835 | Doi | 10.1002/eji.200526323 |
| Citation | Boes M, et al. (2005) In vivo control of endosomal architecture by class II-associated invariant chain and cathepsin S. Eur J Immunol 35(9):2552-62 |
| abstractText | 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. |
