Schematic representation of adenovirus-induced effects on dynein-mediated lyso/LE distribution and mechanism of PKA-mediated effects. (A) At basal PKA activity levels in uninfected cells, lyso/LE cluster around the centrosome. At the onset of infection, adenovirus binds integrins, increasing cAMP levels and PKA activity. PKA phosphorylation of the dynein LIC1 subunit promotes virus transport to the centrosome and nucleus, while dispersing lyso/LEs in a novel mechanism for host–virus competition. (B) Dephosphorylated LIC1 mediates dynein recruitment to the lyso/LEs surface protein RILP, which is, in turn, recruited by activated Rab7. Upon infection, adenovirus–integrin binding leads to cAMP synthesis and PKA activation. LIC1 phosphorylation results in dynein switching from RILP to the virus capsid subunit hexon. Additional factors proposed to contribute to dynein recruitment to lyso/LEs are not depicted here but are described in the Discussion.