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

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PLD2 forms a functional complex with mTOR/raptor to transduce mitogenic signals

Cited 30 times inthomson ciCited 41 times inthomson ci
Title
PLD2 forms a functional complex with mTOR/raptor to transduce mitogenic signals
Author
Ha, Sang HoonKim, Do-HyungKim, Il-ShinKim, Jung HwanLee, Mi NamLee, Hyun JuKim, Jong HeonJang, Sung KeySuh, Pann-GhillRyu, Sung Ho
Issue Date
2006-12
Publisher
ELSEVIER SCIENCE INC
Citation
CELLULAR SIGNALLING, v.18, no.12, pp.2283 - 2291
Abstract
Mammalian target-of-rapamycin (mTOR), which is a master controller of cell growth, senses a mitogenic signal in part through the lipid second messenger phosphatidic acid (PA), generated by phospholipase D (PLD). To understand further which isozymes of PLD are involved in this process, we compared the effect of PLD isozymes on mTOR activation. We found that PLD2 has an essential role in mitogen-induced mTOR activation as the siRNA-mediated knockdown of PLD2, not of PLD I, profoundly reduced the phosphorylations of S6K1 and 4EBP1, well-known mTOR effectors. Furthermore, exogenous PA-induced mTOR activation was abrogated by PLD2 knockdown, but not by PLD I knockdown. This abrogation was found to be the result of complex formation between PLD2 and mTOR/raptor. PLD2 possesses a TOS-like motif (Plie-Ght-Val-Gin-Val, a.a. 265269), through which it interacts with raptor independently of the other TOS motif-containing proteins, S6K1 and 4EBP1. PLD2-dependent mTOR activation appears to require PLD2 binding to mTOR/raptor with lipase activity, since lipase-inactive PLD2 cannot trigger mTOR activation despite its ability to interact with mTOR/raptor. Abrogation of mitogen-dependent mTOR activation by PLD2 knockdown was rescued only by wild type PLD2, but not by raptor binding-deficient and lipase-inactive PLD2. Our results demonstrate the importance of localized PA generation for the mitogen-induced activation of mTOR, which is achieved by a specific interaction between PLD2 and mTOR/raptor. (c) 2006 Elsevier Inc. All rights reserved.
URI
https://scholarworks.unist.ac.kr/handle/201301/10122
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33750336370
DOI
10.1016/j.cellsig.2006.05.021
ISSN
0898-6568
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BIO_Journal Papers
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