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Published online
doi:10.1083/jcb.200609061
The Journal of Cell Biology, Vol. 177, No. 2, 343-354
The Rockefeller University Press, 0021-9525 $30.00
© Gauthier et al.
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Article

Early endosomes associated with dynamic F-actin structures are required for late trafficking of H. pylori VacA toxin



Nils C. Gauthier1, Pascale Monzo2, Teresa Gonzalez2, Anne Doye1, Amanda Oldani3, Pierre Gounon5, Vittorio Ricci3, Mireille Cormont2, and Patrice Boquet4

1 Unité 627 and 2 Unité 568, Institut National de la Santé et de la Recherche Medicale, Faculty of Medicine, 06107 Nice, Cedex 02, France
3 Department of Experimental Medicine, Human Physiology Section, University of Pavia, 27100 Pavia, Italy
4 Department of Clinical Bacteriology, Nice University Hospital, 06202 Nice, Cedex 03, France
5 Centre Commun de Microscopie Appliquée, Faculté des Sciences, Université de Nice Sophia-Antipolis, 06108 Nice, Cedex 02, France

Correspondence to Patrice Boquet: boquet.p{at}chu-nice.fr

Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are endocytosed by a clathrin- independent pathway into vesicles named GPI-AP–enriched early endosomal compartments (GEECs). We recently showed that the vacuolating toxin VacA secreted by Helicobacter pylori is endocytosed into the GEECs (Gauthier, N.C., P. Monzo, V. Kaddai, A. Doye, V. Ricci, and P. Boquet. 2005. Mol. Biol. Cell. 16:4852–4866). Unlike GPI-APs that are mostly recycled back to the plasma membrane, VacA reaches early endosomes (EEs) and then late endosomes (LEs), where vacuolation occurs.

In this study, we used VacA to study the trafficking pathway between GEECs and LEs. We found that VacA routing from GEECs to LEs required polymerized actin. During this trafficking, VacA was transferred from GEECs to EEs associated with polymerized actin structures. The CD2-associated protein (CD2AP), a docking protein implicated in intracellular trafficking, bridged the filamentous actin (F-actin) structures with EEs containing VacA. CD2AP regulated those F-actin structures and was required to transfer VacA from GEECs to LEs. These results demonstrate that sorting from GEECs to LEs requires dynamic F-actin structures on EEs.

N.C. Gauthier and P. Monzo contributed equally to this paper.

N.C. Gauthier's present address is Dept. of Cell Biology, Columbia University, New York, NY 10027.

P. Monzo's present address is Dept. of Pathology, Columbia University, New York, NY 10032.

Abbreviations used in this paper: CD, cytochalasin D; CD2AP, CD2-associated protein; EE, early endosome; EEA1, EE antigen 1; F-actin, filamentous actin; GEEC, GPI-AP–enriched early endosomal compartment; GPI-AP, glycosylphosphatidyl-anchored protein; LAMP1, lysosome-associated membrane protein 1; LE, late endosome; TCR, T cell receptor.


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