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*
Unité Mixte de Recherche, Centre National de la Recherche Scientifique 144, Laboratoire "Mécanismes Moléculaires du Transport Intracellulaire," Institut Curie, Paris, France; and
Contrat Jeune Formation (CJF) INSERM 94-03, Laboratoire d’Histocompatibilité,
INSERM U.311, Etablissement de Transfusion Sanguine, and
§
Service d’Onco-Hématologie, Hopital de Hautepierre, Strasbourg, France
Binding of antigenic peptides to MHC class II (MHC-II) molecules
occurs in the endocytic pathway. From previous studies in B
lymphocytes, it is believed that most but not all of the newly
synthesized MHC-II molecules are directly targeted from the
trans-Golgi network to endosomal compartments. By using
pulse-chase metabolic labeling followed by cell surface biotinylation,
we show here that in contrast to an EBV-transformed B cell line and
human monocytes, the majority of newly synthesized MHC-II molecules (at
least 55 ± 13%) are first routed to the plasma membrane of
dendritic cells derived from human monocytes. They reach the cell
surface in association with the invariant chain (Ii), a polypeptide
known to target MHC-II to the endosomal/lysosomal system. Following
rapid internalization and degradation of Ii, these 
ßIi complexes
are converted into ß-peptide complexes as shown by their SDS
stability. These SDS-stable dimers appear as soon as 15 to 30 min after
internalization of the ßIi complexes. More than 80% of ß
dimers originating from internalized ßIi complexes are
progressively delivered to the cell surface within the next 2 h.
Depolymerization of microtubules, which delays the transport to late
endosomal compartments, did not affect the kinetics of conversion of
surface ßIi into SDS-stable and -unstable ß dimers.
Altogether, these data suggest that newly liberated class II ß
heterodimers may bind peptides in different compartments along the
endocytic pathway in dendritic cells derived from human monocytes.
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