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A role for alpha-and beta-catenins in bacterial uptake.

Abstract : Interaction of internalin with E-cadherin promotes entry of Listeria monocytogenes into human epithelial cells. This process requires actin cytoskeleton rearrangements. Here we show, by using a series of stably transfected cell lines expressing E-cadherin variants, that the ectodomain of E-cadherin is sufficient for bacterial adherence and that the intracytoplasmic domain is required for entry. The critical cytoplasmic region was further mapped to the beta-catenin binding domain. Because beta-catenin is known to interact with alpha-catenin, which binds to actin, we generated a fusion molecule consisting of the ectodomain of E-cadherin and the actin binding site of alpha-catenin. Cells expressing this chimera were as permissive as E-cadherin-expressing cells. In agreement with these data, alpha- and beta-catenins as well as E-cadherin clustered and colocalized at the entry site, where F-actin then accumulated. Taken together, these results reveal that E-cadherin, via beta- and alpha-catenins, can trigger dynamic events of actin polymerization and membrane extensions culminating in bacterial uptake.
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Submitted on : Monday, January 27, 2020 - 3:58:58 PM
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Marc Lecuit, Reini Hurme, Javier Pizarro-Cerdá, Hélène Ohayon, Benjamin Geiger, et al.. A role for alpha-and beta-catenins in bacterial uptake.. Proceedings of the National Academy of Sciences of the United States of America, 2000, 97 (18), pp.10008-10013. ⟨10.1073/pnas.97.18.10008⟩. ⟨pasteur-02456819⟩



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