FERM domain-containing protein FRMD5 regulates cell motility via binding to integrin β5 subunit and ROCK1.

FRMD5 is a novel FERM domain-containing protein depicted in tumor progression. However, the mechanisms underlying FRMD5 inhibition of cell migration is largely unknown. Here, we show that FRMD5 regulates cell migration by interacting with integrin β5 cytoplasmic tail and ROCK1 in human lung cancer cells. FRMD5 promotes cell-matrix adhesion and cell spreading on vitronectin, and thus inhibits cell migration. Furthermore, FRMD5 interacts with ROCK1 and inhibits its activation that leads to the inhibition of myosin light chain phosphorylation and the actin stress fiber formation. Taken together, these findings demonstrate that the putative tumor suppressive protein FRMD5 regulates tumor cell motility via a dual pathway involving FRMD5 binding to integrin β5 tail and to ROCK1.