TRIP6 is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.Deconvolution microscopy demonstrated diffuse cytoplasmic colocalization of srfH and Trip6 in murine macrophages. Bacteria lacking SrfH were unable to stimulate TRIP6-dependent phagocyte migration in vitro or in vivo. Mice lacking Cd18 and infected with Salmonella did not show phagocyte migration, in spite of diminished bactericidal function.