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mTOR phosphorylated at S2448 binds to raptor and rictor

机译：在S2448处磷酸化的mTOR与猛禽和蓖麻结合

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摘要

In mammalian cells, the mammalian target of rapamycin (mTOR) forms an enzyme complex with raptor (together with other proteins) named mTOR complex 1 (mTORCl), of which a major target is the p70 ribosomal protein S6 kinase (p70S6K). A second enzyme complex, mTOR complex 2 (mTORC2), contains mTOR and rictor and regulates the Akt kinase. Both mTORCl and mTORC2 are regulated by phosphorylation, complex formation and localization. So far, the role of p70S6K-mediated mTOR S2448 phosphorylation has not been investigated in detail. Here, we report that endogenous mTOR phosphorylated at S2448 binds to both, raptor and rictor. Experiments with chemical inhibitors of the mTOR kinase and of the phos-phatidylinositol-3-kinase revealed that downregulation of mTOR S2448 phosphorylation correlates with decreased mTORCl activity but can occur decoupled of effects on mTORC2 activity. In addition, we found that the correlation of the mTOR S2448 phosphorylation status with mTORCl activity is not a consequence of effects on the assembly of mTOR protein and raptor. Our data allow new insights into the role of mTOR phosphorylation for the regulation of its kinase activity.
机译：在哺乳动物细胞中，雷帕霉素的哺乳动物靶标（mTOR）与猛禽形成酶复合物（与其他蛋白质一起），称为mTOR复合物1（mTORC1），其主要靶标是p70核糖体蛋白S6激酶（p70S6K）。第二种酶复合物mTOR复合物2（mTORC2）包含mTOR和rictor，并调节Akt激酶。 mTORC1和mTORC2均受磷酸化，复合物形成和定位的调节。迄今为止，尚未详细研究p​​70S6K介导的mTOR S2448磷酸化的作用。在这里，我们报道在S2448磷酸化的内源性mTOR结合到猛禽和蓖麻。用mTOR激酶和磷酸肌醇3激酶的化学​​抑制剂进行的实验表明，mTOR S2448磷酸化的下调与mTORC1活性降低有关，但对mTORC2活性的影响可能是相互独立的。另外，我们发现mTOR S2448磷酸化状态与mTORC1活性的相关性不是对mTOR蛋白和猛禽装配的影响的结果。我们的数据为mTOR磷酸化对其激酶活性的调节作用提供了新的见解。

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