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Vol. 14, Issue 5, 2029-2040, May 2003
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* Max-Planck-Institut für Biologie, Abteilung Membranbiochemie, D-72076
Tübingen, Germany;
Ludwigs-Maximilians-Universität München, Department Biologie I,
Bereich Genetik, D-80638 München, Germany;
Max-Planck-Institut für Entwicklungsbiologie, D-72076 Tübingen,
Germany;
Zentrum für Molekularbiologie der Pflanzen, Universität
Tübingen, D-72076 Tübingen, Germany; and
|| Wellcome Trust Laboratories for Molecular Parasitology, Imperial College
London, Department of Biological Sciences and Centre for Molecular
Microbiology and Infection, London, SW7 2AY, United Kingdom
Submitted October 10, 2002; Revised December 3, 2002; Monitoring Editor: Jennifer-Lippincott-Schwartz
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 with 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 in 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 in 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 in diameter, 34 nm in thickness), which are shown to fuse with the flagellar pocket membrane, thereby recycling VSG back to the cell surface.
Abbreviations used: GPI, glycosylphosphatidylinositol; VSG, variant surface glycoprotein; AMCA, 7-amino-4-methylcoumarin; FP, flagellar pocket; CCV, clathrin-coated vesicle; EC, endosomal cisterna; EXC, exocytic carrier vesicle; PAG, protein A gold complex.
Online version of this article contains video material. Online version of
this article is available at
www.molbiolcell.org.
¶ Corresponding author. E-mail address: peter.overath{at}tuebingen.mpg.de.
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