Osmotic Stress Regulates Mammalian Target of Rapamycin (mTOR) Complex 1 via c-Jun N-terminal Kinase (JNK)-mediated Raptor Protein Phosphorylation
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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
- Kwak, Dongoh; Choi, Sunkyu; Jeong, Heeyoon; Jang, Jin-Hyeok; Lee, Youngmi; Jeon, Hyeona; Lee, Mi Nam; Noh, Jungeun; Cho, Kun; Yoo, Jong Shin; Hwang, Daehee; Suh, Pann-Ghill; Ryu, Sung Ho
- C-jun N-terminal kinase; Complex 1; Control-cell; Essential component; Growth factor; In-vitro; Kinase activity; Liquid chromatography-tandem mass spectrometry; Mammalian target of rapamycin (mTOR); Molecular links; Multi-protein complex; Osmotic stress; Potential mechanism; Protein phosphorylation; Signaling pathways
- Issue Date
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- JOURNAL OF BIOLOGICAL CHEMISTRY, v.287, no.22, pp.18398 - 18407
- 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.
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