AI Article Synopsis
- GPI-anchored proteins (GPI-APs) enter cells through a clathrin-independent pathway, leading to specialized vesicles called GEECs, and VacA from Helicobacter pylori also follows this pathway.
- Unlike typical GPI-APs that are recycled back to the surface, VacA progresses to early endosomes (EEs) and late endosomes (LEs) where it causes vacuolation.
- The routing of VacA from GEECs to LEs is dependent on polymerized actin and requires the CD2-associated protein (CD2AP), which helps facilitate the transfer between these compartments.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064141 | PMC |
| http://dx.doi.org/10.1083/jcb.200609061 | DOI Listing |
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