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J. Biol. Chem., Vol. 276, Issue 16, 13469-13475, April 20, 2001
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From the Section of Immunobiology, University of Bonn, 53117 Bonn,
Römerstrasse 164, Germany
Invariant chain (Ii) serves as a chaperone
for folding and intracellular transport of major histocompatibility
complex class II (MHCII) molecules. Early in biosynthesis, Ii
associates with MHCII molecules and directs their intracellular
transport to endocytic compartments where vesicular proteinases
sequentially release Ii from the MHCII heterodimer. The detachment of
Ii makes the MHCII groove susceptible for binding of antigenic
peptides. We investigated the role of N-linked
glycosylation in the controlled intracellular degradation of Ii. Motifs
for asparagine-linked glycosylation were altered, and mutated Ii
(IiNmut) was transiently expressed in COS cells. The half-life of
IiNmut was strongly reduced compared with wild-type Ii although the
sensitivity of the N glycan-free polypeptide to in
vitro proteinase digestion was not substantially increased.
Inhibition of vesicular proteinases revealed endosomal degradation of
IiNmut. Intracellular proteolysis of IiNmut is substantially impaired
by serine proteinase inhibitors. Thus, a considerable amount of IiNmut
is degraded in nonacidic intracellular compartments. The data
suggest that N-linked glycosylation of Ii hinders premature
proteolysis in nonacidic vesicles resulting in Ii degradation in acidic
MHC class II-processing compartments.
Glycosylation Signals That Separate the Trimerization from the
MHC Class II-binding Domain Control Intracellular Degradation of
Invariant Chain*
*
This work was supported by the Sonderforschungsbereich 284, Teilprojekt B6.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 0049 228 734343;
Fax: 0049 228 734555; E-mail: norbert.koch@uni-bonn.de.
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