Bacterial pathogens recruit clathrin upon interaction with host surface 
receptors during infection. Here, using three different infection models, we 
observed that host-pathogen interactions induce tyrosine phosphorylation of 
clathrin heavy chain. This modification was critical for recruitment of actin at 
bacteria-host adhesion sites during bacterial internalization or pedestal 
formation. At the bacterial interface, clathrin assembled to form coated pits of 
conventional size. Because such structures cannot internalize large particles 
such as bacteria, we propose that during infection, clathrin-coated pits serve 
as platforms to initiate actin rearrangements at bacteria-host adhesion sites. 
We then showed that the clathrin-actin interdependency is initiated by Dab2 and 
depends on the presence of clathrin light chain and its actin-binding partner 
Hip1R, and that the fully assembled machinery can recruit Myosin VI. Together, 
our study highlights a physiological role for clathrin heavy chain 
phosphorylation and reinforces the increasingly recognized function of clathrin 
in actin cytoskeletal organization in mammalian cells.