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A more recent version of this article appeared on January 1, 2002 Originally published as MBC in Press, 10.1091/mbc.01-06-0300 on December 7, 2001
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Submitted on June 20, 2001
Revised on October 11, 2001
Accepted on October 31, 2001
1 UMR 144 CNRS-Institut Curie, Laboratoire "Mecanismes Moleculaires du Transport Intracellulaire", Paris, France
2 INSERM EP 99-08 "Biologie des Cellules Dendritiques Humaines", Alsace, 67065 Strasbourg Cedex, France
3 Department of Dermatology and Center for Electron Microscopy, LUMC, 2300 RA Leiden, The Netherlands
4 INSERM U 311, Etablissement Francais du Sang - Alsace, 67065 Strasbourg Cedex, France
5 Laboratoire de Microscopie Electronique, Institut Curie, 26 rue d'Ulm, Paris, France
6 UMR 144 CNRS-Institut Curie, Laboratoire "Mecanismes Moleculaires du Transport Intracellulaire", Paris, France
* Corresponding author. E-mail address: daniel.hanau{at}efs-alsace.fr.
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 internalises 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, while 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 which form where Langerin accumulates. Finally, our results implicate Arf proteins in Langerin trafficking and the exchange between Birbeck granules and other endosomal membranes.
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