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• W2015489095 abstract "mTORC2, the mammalian target of rapamycin complex 2 is activated by upstream growth factors, and performs two major functions, phosphorylation of AKT at the serine of 473 and cell cycle-dependent organization of actin cytoskeleton. However, the mechanisms through which mTORC2 is triggered by these signals remain unclear. We demonstrated, for the first time, that inhibitor of nuclear factor κ-B kinase (IKK) interacted with rictor and regulated mTORC2 activity. Not only endogenously, but ectopically expressed IKK α and IKK β physically interacted with rictor. An in vitro binding assay revealed that rictor interacted with IKKα and IKKβ from amino acids 999 to 1397. Moreover, chemical inhibition of IKK, knockdown of IKK by small interference RNA (siRNA), or ectopic expression of kinase-dead IKK (IKK KD) repressed phosphorylation of AKT (S473) in a variety of cell lines and decreased the kinase activity of mTORC2. In NIH 3T3 cells, inhibition of IKK also reduced phosphorylation of protein kinase α (PKCα) (S657) and resulted in disorganization of actin cytoskeleton. Interestingly, the interaction between IKKα/β and rictor was increased, while the mTOR-rictor association was attenuated by inhibition of IKK. We identified a novel signaling mechanism for the regulation of mTORC2 by IKK: IKK interacted with rictor and regulated the function of mTORC2 including phosphorylation of AKT (S473) and organization of actin cytoskeleton. Inactivated IKK interacted with rictor and competed against mTOR, which resulted in a reduced mTORC2 level and a decrease in mTORC2 activity." @default.
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• W2015489095 date "2013-11-01" @default.
• W2015489095 modified "2023-10-14" @default.
• W2015489095 title "IKK interacts with rictor and regulates mTORC2" @default.
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• W2015489095 doi "https://doi.org/10.1016/j.cellsig.2013.07.008" @default.
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