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  • Title: Expression of major histocompatibility complex class II molecules in HeLa cells promotes the recruitment of AP-1 Golgi-specific assembly proteins on Golgi membranes.
    Author: Salamero J, Le Borgne R, Saudrais C, Goud B, Hoflack B.
    Journal: J Biol Chem; 1996 Nov 29; 271(48):30318-21. PubMed ID: 8939989.
    Abstract:
    The newly synthesized major histocompatibility complex (MHC) class II molecules, an alphabeta 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 alphabetaIi 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, alphabeta 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 alphabeta 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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