Birbeck Granules Are Subdomains of Endosomal Recycling Compartment in Human Epidermal Langerhans Cells, Which Form Where Langerin Accumulates

Author:

Mc Dermott Ray1,Ziylan Umit2,Spehner Danièle2,Bausinger Huguette2,Lipsker Dan2,Mommaas Mieke3,Cazenave Jean-Pierre4,Raposo Graça5,Goud Bruno1,de la Salle Henri2,Salamero Jean1,Hanau Daniel2

Affiliation:

1. Unité Mixte de Recherche 144 Centre National de laRecherche Scientifique-Institut Curie, Laboratoire Mécanismes Moléculaires du Transport Intracellulaire and

2. Institut National de la Santéet de la Recherche Médicale EP 99–08 Biologie des Cellules Dendritiques Humaines and

3. Department of Dermatology and Center for Electron Microscopy, Leidem University Medical Center, 2300 RA Leiden, The Netherlands

4. Institut National de la Santé et de la Recherche Médicale U 311, Etablissement Français du Sang-Alsace, 67065 Strasbourg, France; and

5. Laboratoire de Microscopie Electronique, Institut Curie, 75248 Paris, France;

Abstract

Birbeck granules are unusual rod-shaped structures specific to epidermal Langerhans cells, whose origin and function remain undetermined. We investigated the intracellular location and fate of Langerin, a protein implicated in Birbeck granule biogenesis, in human epidermal Langerhans cells. In the steady state, Langerin is predominantly found in the endosomal recycling compartment and in Birbeck granules. Langerin internalizes by classical receptor-mediated endocytosis and the first Birbeck granules accessible to endocytosed Langerin are those connected to recycling endosomes in the pericentriolar area, where Langerin accumulates. Drug-induced inhibition of endocytosis results in the appearance of abundant open-ended Birbeck granule-like structures appended to the plasma membrane, whereas inhibition of recycling induces Birbeck granules to merge with a tubular endosomal network. In mature Langerhans cells, Langerin traffic is abolished and the loss of internal Langerin is associated with a concomitant depletion of Birbeck granules. Our results demonstrate an exchange of Langerin between early endosomal compartments and the plasma membrane, with dynamic retention in the endosomal recycling compartment. They show that Birbeck granules are not endocytotic structures, rather they are subdomains of the endosomal recycling compartment that form where Langerin accumulates. Finally, our results implicate ADP-ribosylation factor proteins in Langerin trafficking and the exchange between Birbeck granules and other endosomal membranes.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

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