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

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.

journal_name

Eur J Immunol

authors

Boes M,van der Wel N,Peperzak V,Kim YM,Peters PJ,Ploegh H

doi

10.1002/eji.200526323

keywords:

subject

Has Abstract

pub_date

2005-09-01 00:00:00

pages

2552-62

issue

9

eissn

0014-2980

issn

1521-4141

journal_volume

35

pub_type

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