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Biologie cellulaire de l'infection par <i>Listeria monocytogenes</i>

Dynamics of the InlA/E-cadherin interaction.

J. Pizarro-Cerda et al. (2010) Bioessays 32:496-504 Entry of L. monocytogenes via the InlA/E-cadherin interaction. (A) The bacterial protein InlA interacts with its lipid raft-associated receptor E-cadherin to promote the recruitment to the bacterial entry site of several members of the catenin family including p120, b-and a-catenin. (B) Caveolin-1 participates in the clustering of E-cadherin and in the activation of Src, which in turn phosphorylates E-cadherin. (C) E-cadherin phosphorylation triggers the ubiquitination of the receptor by the ubiquitin-ligase Hakai which is required for the subsequent recruitment of clathrin. (D) Src is also involved in the phosphorylation of cortactin, which promotes Arp2/3 complex activation and actin polymerization.