ZBP1-modulated localization of β-actin mRNA enables a cell to establish polarity and structural asymmetry. While the mechanism of β-actin mRNA localization has been well revealed, the underlying mechanism of how a specific molecular motor contributes to transport of the ZBP1 complex in non-neuronal cells remains elusive. In this study, we report the isolation and identification of KIF11, a microtubule motor, which physically interacts with ZBP1 and is a component of β-actin mRNP. We show that KIF11 co-localizes with the β-actin mRNA and the ability of KIF11 to transport β-actin mRNA is ZBP1-dependent. We characterize the corresponding regions of ZBP1 and KIF11, which mediate the two protein's interaction in vitro and in vivo. Disruption of the in vivo interaction of KIF11 with ZBP1 delocalizes β-actin mRNA and affects cell migration. Our study reveals a molecular mechanism that a particular microtubule motor mediates the transport of an mRNP through the direct interaction with an mRNA-binding protein.