We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Early endosomes associated with dynamic F-actin structures are required for late trafficking of H. pylori VacA toxin.
- Authors
Gauthier, Nils C.; Monzo, Pascale; Gonzalez, Teresa; Doye, Anne; Oldani, Amanda; Gounon, Pierre; Ricci, Vittoria; Cormont, Mireille; Boquet, Patrice; Gauthier, N. C.; Monzo, P.
- Abstract
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.
- Subjects
ENDOSOMES; ACTIN; TOXINS; PROTEINS; ENDOCYTOSIS
- Publication
Journal of Cell Biology, 2007, Vol 177, Issue 2, p343
- ISSN
0021-9525
- Publication type
Article
- DOI
10.1083/jcb.200609061