Timely activation of Aurora Kinase A (AURA) is vital for centrosome formation and the progression of mitosis. Nonetheless, it is still unclear if and when other cellular functions are activated by AURA. We report here that Src phosphorylates and activates AURA at T288 and AURA also activates focal adhesion kinase (FAK), leading to initiation of cell movement. An additional and new way by which AURA is regulated, is by phospholipase D (PLD) that causes AURA activation. Conversely, AURA phosphorylates PLD, so both proteins engage in a positive reinforcement loop. AURA and PLD2 form a protein-protein complex and co-localize to cytoplasmic regions in cells. The reason why PLD activates AURA is because of the production of phosphatidic acid (PA) by the lipase that binds directly to AURA, with the region E171–E211 projected to be a PA binding pocket. Further, this direct interaction with PA enhances actin polymerization and cooperates synergistically with AURA, FAK and Src in yielding a fully effectual cellular migration. Thus, Src/FAK and PLD/PA are novel upstream regulators of AURA during the non-mitotic cellular function of cell migration.