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Volume 272, Number 13, Issue of March 28, 1997 pp. 8281-8287
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Exon 6 Is Essential for Invariant Chain Trimerization and Induction of Large Endosomal Structures

(Received for publication, September 11, 1996, and in revised form, January 13, 1997)

Merete Gedde-Dahl , Ina Freisewinkel § , Michael Staschewski § , Klaus Schenck , Norbert Koch § and Oddmund Bakke

From the Division of Molecular Cell Biology, Department of Biology, University of Oslo, N-0316 Oslo, Norway and the § Section of Immunobiology, Institute of Zoology, University of Bonn, Römerstrasse 164, D-53117 Bonn, Germany

Invariant chain (Ii) is a transmembrane type II protein that forms a complex with the major histocompatibility complex (MHC) class II molecules in the endoplasmic reticulum (ER). The membrane proximal luminal region of Ii is responsible for the non-covalent association with MHC class II molecules. Chemical cross-linking in COS cells was used to study the effect of luminal and cytoplasmic deletions on trimerization of Ii. We demonstrate that trimerization of Ii is independent of the cytosolic tail of Ii, whereas residues 162-191 (the sequence encoded by exon 6) in the luminal part of Ii are essential for trimer formation. Immunofluorescence studies of the transfected luminal deletion constructs show that the amino acids encoded by exon 6 of Ii are also essential for the induction of large endosomal vesicles. The data suggest that Ii must be in a trimeric form to modify the endosomal pathway.


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