LAUSR

EphB2/ephrinB signalling that plays a major role in cell segregation during embryonic development and tissue homeostasis, induces an important reorganization of the cortical actin network. We have previously reported that myosin 1b contributes to the reorganisation of the cortical actin network upon EphB2 signalling. In this report we have identified Plekhh1, as a new partner of members of the myosin 1 family and EphB2 receptors. Plekhh1 interacts with myosin 1b via its N-terminus domain and with EphB2 via its C-terminus domain. Furthermore, Plekhh1 is tyrosine-phosphorylated, and this depends on EphB2 kinase activity. Such as the manipulation of the expression level of myosin 1b and myosin 1c, manipulation of Plekhh1 expression levels reveals that Plekhh1 controls the formation of filopodia, the length of focal adhesions and the formation of blebs. Furthermore, binding of Plekhh1 interacting domain to myosin 1b increases the motor activity of myosin 1b in vitro. Together our data show that Plekhh1 is an effector of EphB2 and suggest that Plekhh1 regulates the cortical actin network via the interaction of its N-terminus domain with myosin 1 upon EphB2/ephrinB signalling.