Letter abstract
Nature Cell Biology 7, 954 - 960 (2005)
Published online: 25 September 2005 | doi:10.1038/ncb1308
ARHGAP10 is necessary for 
-catenin recruitment at adherens junctions and for Listeria invasion
Sandra Sousa1,6, Didier Cabanes1,6, Cristel Archambaud1, Frédéric Colland2, Emmanuel Lemichez3, Michel Popoff4, Stéphanie Boisson-Dupuis1, Edith Gouin1, Marc Lecuit1,5, Pierre Legrain3,7 & Pascale Cossart1
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 
-catenin, which then recruits 
-catenin. -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 -catenin. Using a two-hybrid screen, we identified a new partner of -catenin: ARHGAP10. This protein colocalized with -catenin at cell–cell junctions and was recruited at L. monocytogenes entry sites. In ARHGAP10-knockdown cells, L. monocytogenes entry and -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 -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 -catenin recruitment and has a key role during L. monocytogenes uptake.
- Unité des Interactions Bactéries-Cellules Institut Pasteur, INSERM U604, INRA USC2020, 28 Rue du Dr Roux, 75724 Paris Cedex 15, France.
- Hybrigenics SA, 3-5 Impasse Reille, 75014 Paris, France.
- Bacterial toxins in host-pathogen interaction, Faculté de Médecine de Nice, 28 Avenue de Valombrose, Nice 06107 Cedex 02, France.
- Unité Bacteries anaerobies et Toxines Institut Pasteur, Paris.
- Service des Maladies Infectieuses et Tropicales, Hôpital Necker-Enfants Malades, 149 rue de Sèvres, 75015 Paris, France.
- Present addresses: Institute for Molecular and Cell Biology, Molecular Microbiology, Rua do Campo Alegre 823, 4150-180 Porto, Portugal;
- Département de Biologie Joliot-Curie, CEA, 91191 Gif-sur-Yvette CEDEX, France.
Correspondence to: Pascale Cossart1 e-mail: pcossart@pasteur.fr
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