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Volume 271, Number 48, Issue of November 29, 1996 pp. 30318-30321
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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COMMUNICATION:
Expression of Major Histocompatibility Complex Class II Molecules in HeLa Cells Promotes the Recruitment of AP-1 Golgi-specific Assembly Proteins on Golgi Membranes

(Received for publication, August 19, 1996, and in revised form, October 14, 1996)

Jean Salamero , Roland Le Borgne ^§ , Cedric Saudrais , Bruno Goud and Bernard Hoflack ^§

From ^§ EMBL, Postfach 10-2209, Meyerhofstrasse 1, D-69012 Heidelberg, Germany and  UMR 144 CNRS- Institut Curie, Laboratoire "Mecanismes Moléculaires du Transport Intracellulaire, 12 rue Lhomond, 75005 Paris, France

The newly synthesized major histocompatibility complex (MHC) class II molecules, an dimer associated with the Ii invariant chain, must be targeted to endosomal, lysosomal enzyme-rich compartments in order to bind and present immunogenic peptides. The precise route followed by this complex at the exit of the trans-Golgi network, the last sorting station of the biosynthetic pathway, is poorly understood. We show here that overexpression of Ii complexes in HeLa cells promotes the first step of clathrin-coat assembly in vitro, that is the ARF-dependent translocation of AP-1 Golgi-specific assembly proteins on membranes. In contrast, dimers alone or associated with Ii lacking most of its cytoplasmic domain fail to recruit AP-1. This study strongly suggests that the invariant chain (Ii) is responsible for the AP-1-dependent sorting of the dimers in the trans-Golgi network of HeLa cells and that the MHC class II molecules are, like the mannose 6-phosphate receptors, transported directly from this compartment to endosomes via clathrin-coated vesicles.

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