Images

Figure from Pizarro-Cerda et al. Cell 2006

Invasive Molecular Strategies of Listeria. (D) Listeria invades target cells combining two molecular pathways. In the InlA-dependent pathway, the sortase-anchored bacterial protein InlA interacts with the cell adhesion molecule E-cadherin and promotes the subversion of cell adherens junction machinery (including b- and a-catenins) to induce entry. The myosin VIIA probably generates the contractile force required for bacterial engulfment. Actin polymerization relies, among other molecules, on the RhoGTPase Rac1. In the InlB-dependent pathway, the loosely cell wall-attached bacterial protein InlB interacts with the molecule gC1qR, and with the signaling receptor Met, which recruits several molecular adaptors, which will perform several function including the recruitment of a PI3K (involved in the activation of the RhoGTPase Rac1 and the polymerization of actin), and also the ubiquitination of Met and the endocytosis of the receptor via a clathrin-dependent mechanisms. A balance between actin polymerization and actin depolymerization required for efficient bacterial entry is controlled by regulation of the activities of the Lim kinase and the actin depolymerizing factor cofilin.