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Pyruvate Kinase M2 Activates mTORC1 by Phosphorylating AKT1S1 期刊论文

编号：

d6fe7159-bc67-4620-a458-08f94b6dccc3
作者：

He, ChangLiang^[1,2,3,4,7];Bian, YangYang^[5];Xue, Yu^[6];Liu, ZeXian^[6];Zhou, KaiQiang^[1,2,3,4];Yao, CuiFang^[1,2,3,4];Lin, Yan(林彦)^[1,2,3,4]Zou, HanFa^[5];Luo, FangXiu^[8];Qu, YuanYuan(瞿元元)^[9,10]Zhao, JianYuan^[1,2,7];Ye, MingLiang^[5];Zhao, ShiMin(赵世民)*^[1,2,3,4,7]Xu, Wei^[1,2,3,4,7];
语种：

英文
期刊：

SCIENTIFIC REPORTS ISSN：2045-2322 2016 年 6 卷 ; FEB 15
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摘要：

In cancer cells, the mammalian target of rapamycin complex 1 (mTORC1) that requires hormonal and nutrient signals for its activation, is constitutively activated. We found that overexpression of pyruvate kinase M2 (PKM2) activates mTORC1 signaling through phosphorylating mTORC1 inhibitor AKT1 substrate 1 (AKT1S1). An unbiased quantitative phosphoproteomic survey identified 974 PKM2 substrates, including serine202 and serine203 (S202/203) of AKT1S1, in the proteome of renal cell carcinoma (RCC). Phosphorylation of S202/203 of AKT1S1 by PKM2 released AKT1S1 from raptor and facilitated its binding to 14-3-3, resulted in hormonal-and nutrient-signals independent activation of mTORC1 signaling and led accelerated oncogenic growth and autophagy inhibition in cancer cells. Decreasing S202/203 phosphorylation by TEPP-46 treatment reversed these effects. In RCCs and breast cancers, PKM2 overexpression was correlated with elevated S202/203 phosphorylation, activated mTORC1 and inhibited autophagy. Our results provided the first phosphorylome of PKM2 and revealed a constitutive mTORC1 activating mechanism in cancer cells.
推荐引用方式
GB/T 7714：

He Chang-Liang,Bian Yang-Yang,Xue Yu, et al. Pyruvate Kinase M2 Activates mTORC1 by Phosphorylating AKT1S1 [J].SCIENTIFIC REPORTS,2016,6.
APA：

He Chang-Liang,Bian Yang-Yang,Xue Yu,Liu Ze-Xian,&Xu Wei.(2016).Pyruvate Kinase M2 Activates mTORC1 by Phosphorylating AKT1S1 .SCIENTIFIC REPORTS,6.
MLA：

He Chang-Liang, et al. "Pyruvate Kinase M2 Activates mTORC1 by Phosphorylating AKT1S1" .SCIENTIFIC REPORTS 6(2016).
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