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Osmotic Stress Regulates Mammalian Target of Rapamycin (mTOR) Complex 1 via c-Jun N-terminal Kinase (JNK)-mediated Raptor Protein Phosphorylation

Title
Osmotic Stress Regulates Mammalian Target of Rapamycin (mTOR) Complex 1 via c-Jun N-terminal Kinase (JNK)-mediated Raptor Protein Phosphorylation
Authors
Kwak, DChoi, SJeong, HJang, JHLee, YJeon, HLee, MNNoh, JCho, KYoo, JSHwang, DSuh, PGRyu, SH
POSTECH Authors
Hwang, D
Date Issued
May-2012
Publisher
JOURNAL OF BIOLOGICAL CHEMISTRY
Abstract
mTOR complex 1 (mTORC1) is a multiprotein complex that integrates diverse signals including growth factors, nutrients, and stress to control cell growth. Raptor is an essential component of mTORC1 that functions to recruit specific substrates. Recently, Raptor was suggested to be a key target of regulation of mTORC1. Here, we show that Raptor is phosphorylated by JNK upon osmotic stress. We identified that osmotic stress induces the phosphorylation of Raptor at Ser-696, Thr-706, and Ser-863 using liquid chromatography-tandem mass spectrometry. We found that JNK is responsible for the phosphorylation. The inhibition of JNK abolishes the phosphorylation of Raptor induced by osmotic stress in cells. Furthermore, JNK physically associates with Raptor and phosphorylates Raptor in vitro, implying that JNK is responsible for the phosphorylation of Raptor. Finally, we found that osmotic stress activates mTORC1 kinase activity in a JNK-dependent manner. Our findings suggest that the molecular link between JNK and Raptor is a potential mechanism by which stress regulates the mTORC1 signaling pathway.
Keywords
SIGNAL-TRANSDUCTION; CELL-GROWTH; S6 KINASE; ACTIVATION; PATHWAY; TOR; PHOSPHATASE; MECHANISMS; INTERACTS; P70(S6K)
URI
http://oasis.postech.ac.kr/handle/2014.oak/16164
DOI
10.1074/JBC.M111.326
ISSN
0021-9258
Article Type
Article
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 287, no. 22, page. 18398 - 18407, 2012-05
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 HWANG, DAEHEE
Div of Integrative Biosci & Biotech
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