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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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

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Title
GTP-dependent interaction between phospholipase D and dynamin modulates fibronectin-induced cell spreading
Author
Lee, Chang SupKim, Jong MinGhim, JaewangSuh, Pann-GhillRyu, Sung Ho
Issue Date
2015-12
Publisher
ELSEVIER SCIENCE INC
Citation
CELLULAR SIGNALLING, v.27, no.12, pp.2363 - 2370
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 didn't have GAP activity increased the GTP-dependent interaction between PLD and dynamin; it also increased PLD activity and cell spreading. These findings suggest that the observed increase in PLD activity was through boosting the binding of PLD with dynamin and it facilitated FN-induced cell spreading. These results imply that GTP-loaded dynamin, like a small GTPase could mediate a "switch on" signaling via interaction with PLD that has a role as an effector. (C) 2015 Elsevier Inc. All rights reserved
URI
https://scholarworks.unist.ac.kr/handle/201301/18203
URL
http://www.sciencedirect.com/science/article/pii/S0898656815002508
DOI
10.1016/j.cellsig.2015.08.019
ISSN
0898-6568
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BIO_Journal Papers
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