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A more recent version of this article appeared on May 1, 2003
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Submitted on October 10, 2002
Revised on December 3, 2002
Accepted on January 23, 2003
1 Max-Planck-Institut für Biologie, Abteilung Membranbiochemie, Corrensstrasse 38, D-72076 Tübingen, Germany
2 Ludwigs-Maximilians-Universität München, Department Biologie I, Bereich Genetik, Maria-Ward-Strasse 1a, D-80638 München, Germany
3 Max-Planck-Institut für Entwicklungsbiologie, Spemannstrasse 35, D-72076 Tübingen, Germany
4 Zentrum für Molekularbiologie der Pflanzen, Universität Tübingen, Auf der Morgenstelle, D-72076 Tübingen, Germany
5 Wellcome Trust Laboratories for Molecular Parasitology, Imperial College London, Department of Biological Sciences and Centre for Molecular Microbiology and Infection, Exhibition Road, London, SW7 2AY, UK
* Corresponding author. E-mail address: peter.overath{at}tuebingen.mpg.de.
Recently, proteins linked to glycosylphosphatidylinositol (GPI) residues have received considerable attention both for their association with lipid microdomains and for their specific transport between cellular membranes. Basic features of trafficking of GPI-anchored proteins or glycolipids may be explored in flagellated protozoan parasites, which offer the advantage that their surface is dominated by these components. In Trypanosoma brucei, the GPI-anchored variant surface glycoprotein (VSG) is efficiently sorted at multiple intracellular levels leading to a 50-fold higher membrane concentration at the cell surface compared to the endoplasmic reticulum. We have studied the membrane and VSG flow at an invagination of the plasma membrane, the flagellar pocket, the sole region for endo- and exocytosis in this organism. VSG enters trypanosomes in large clathrin-coated vesicles (135 nm diameter), which deliver their cargo to endosomes. In the lumen of cisternal endosomes, VSG is concentrated by default, because a distinct class of small clathrin-coated vesicles (50-60 nm diameter) budding from the cisternae is depleted in VSG. TbRAB11-positive cisternal endosomes, containing VSG, fragment by an unknown process giving rise to intensely TbRAB11- as well as VSG-positive, disk-like carriers (154 nm diameter, thickness 34 nm), which are shown to fuse with the flagellar pocket membrane, thereby recycling VSG back to the cell surface.
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