GTP-dependent interaction between phospholipase D and dynamin modulates fibronectin-induced cell spreading

Cellular Signalling
Chang Sup LeeSung Ho Ryu

Abstract

Phospholipase D (PLD) is one of the key enzymes to mediate a variety of cellular phenomena including endocytosis, actin rearrangement, proliferation, differentiation, and migration. Dynamin as a PLD-interacting partner is a large GTP binding protein that has been considered a mechanochemical enzyme involved in endocytosis by hydrolyzing GTP. Although both PLD and dynamin have been implicated in the regulation of actin cytoskeleton, it is not known how they have a link to regulate fibronectin (FN)-induced cell spreading. Furthermore, it is unknown whether dynamin can work as a GTP-dependent regulator through its interaction with other proteins. Here, we demonstrate that PLD can be regulated by dynamin in a GTP-dependent manner and that this is critical for FN-mediated cell spreading. First, we verified that GTP-loaded dynamin can mediate the cell spreading by FN by using dynamin's GTP binding deficient mutant (K44A). Also, we confirmed that blocking the PLD activity inhibited FN-induced cell spreading, not cell adhesion. Moreover, PLD interacted with dynamin in a GTP-dependent manner in FN signaling, and this interaction was crucial for FN-induced PLD activation and cell spreading. Also, we found that PLD mutant (R128K) that did...Continue Reading

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