Human phosphatase CDC14A is recruited to the cell leading edge to regulate cell migration and adhesion

Abstract

Significance Cell migration and adhesion play critical roles in animal development and tumor metastasis and are regulated by protein phosphorylation. Here we identified the human phosphatase hCDC14A (human cell-division cycle 14A) as F-actin binding protein at the leading edge that regulates both processes. Loss of hCDC14A activity promotes cell mobility and reduces cell adhesion. Importantly, cells devoid of hCDC14A activity were more invasive in a colony-forming assay. Database analysis indicates that hCDC14A expression is frequently down-regulated in cancer tissues and is associated with poor patient prognosis. Thus, the promigratory impact of hCDC14A inactivation upon the F-actin cytoskeleton supports tumor proliferation and metastasis. This hCDC14A function is clearly distinct from the mitotic functions of the budding and fission yeast orthologs Cdc14/Flp1.