Regulation of phospholipase D2 by GTP-dependent interaction with dynamin

Abstract

Phospholipase D (PLD) has been implicated in various cellular events such as vesicle trafficking, cytoskeletal rearrangement, and neurotransmitter release. However, the functional significance of PLD in these processes is still unclear. In this study, we identified dynamin as a PLD2-interacting molecule in rat brain. Dynamin is a GTPase family member and has been implicated in the formation of nascent vesicles in both the endocytic and secretory pathways. Dynamin was found to interact with PLD2 in a GTP-dependent manner, whereas DYN-K44A, a dominant negative mutant of dynamin, did not interact with PLD2. Interaction between dynamin and PLD2 was transient after treatment with EGF, and this was found to correlate with the activation of PLD2. Furthermore, overexpression of the DYN-K44A repressed the EGF induced PLD activity and their interaction in the COS-7 cells. These results suggest that the GTP-dependent interaction of PLD2 and dynamin might play an important role in the EGF-induced PLD activation.