Author: ["Sandra Sousa","Didier Cabanes","Cristel Archambaud","Frédéric Colland","Emmanuel Lemichez","Michel Popoff","Stéphanie Boisson-Dupuis","Edith Gouin","Marc Lecuit","Pierre Legrain","Pascale Cossart"]
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Abstract
E-cadherin mediates the formation of adherens junctions between epithelial cells1. It serves as a receptor for Listeria monocytogenes, a bacterial pathogen that enters epithelial cells2. The L. monocytogenes surface protein, InlA, interacts with the extracellular domain of E-cadherin3,4,5. In adherens junctions, this ectodomain is involved in homophilic interactions whereas the cytoplasmic domain binds β-catenin, which then recruits α-catenin. α-catenin binds to actin directly, or indirectly, thus linking E-cadherin to the actin cytoskeleton6,7. Entry of L. monocytogenes into cells and adherens junction formation are dynamic events that involve actin and membrane rearrangements. To understand these processes better, we searched for new ligands of α-catenin. Using a two-hybrid screen, we identified a new partner of α-catenin: ARHGAP10. This protein colocalized with α-catenin at cell–cell junctions and was recruited at L. monocytogenes entry sites. In ARHGAP10-knockdown cells, L. monocytogenes entry and α-catenin recruitment at cell–cell contacts were impaired. The GAP domain of ARHGAP10 has GAP activity for RhoA and Cdc42. Its overexpression disrupted actin cables, enhanced α-catenin and cortical actin levels at cell–cell junctions and inhibited L. monocytogenes entry. Altogether, our results show that ARHGAP10 is a new component of cell–cell junctions that controls α-catenin recruitment and has a key role during L. monocytogenes uptake.Cite this article
Sousa, S., Cabanes, D., Archambaud, C. et al. ARHGAP10 is necessary for α-catenin recruitment at adherens junctions and for Listeria invasion. Nat Cell Biol 7, 954–960 (2005). https://doi.org/10.1038/ncb1308 