File:Proposed model for C. jejuni-induced signaling leading to Rac1 activation and bacterial invasion.jpg

English: C. jejuni adheres to host cells via the fibronectin-binding protein CadF which acts as a bridge engaging the integrin β1 receptor. Integrin occupancy and clustering in lipid rafts leads to recruitment and activation of the non-receptor tyrosine kinase FAK. Phosphorylation of FAK triggers a cascade of signals resulting in the formation of protein complexes leading to activation of GEFs, including DOCK180 and Tiam-1. Activated DOCK180 and Tiam-1 then induce the activation of Rac1. This potentially causes localized actin and/or microtubule rearrangements at the site of C. jejuni entry, resulting in bacterial uptake. In addition to C. jejuni cadF, some flagellar genes also appear to play a role. If the flagellum participates by sole bacterial motility, by translocating bacterial Cia effector proteins or targeting a host receptor directly is not yet clear.