Pyruvate Kinase M2 Activates mTORC1 by Phosphorylating AKT1S1

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 substr...

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Published inScientific reports Vol. 6; no. 1; p. 21524
Main Authors He, Chang-Liang, Bian, Yang-Yang, Xue, Yu, Liu, Ze-Xian, Zhou, Kai-Qiang, Yao, Cui-Fang, Lin, Yan, Zou, Han-Fa, Luo, Fang-Xiu, Qu, Yuan-Yuan, Zhao, Jian-Yuan, Ye, Ming-Liang, Zhao, Shi-Min, Xu, Wei
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 15.02.2016
Nature Publishing Group
Subjects
13
13/109
13/51
14
14-3-3 protein
14/63
38
38/1
38/70
38/77
631/67/2327
631/80/86
82
82/58
82/80
82/83
Adaptor Proteins, Signal Transducing - biosynthesis
Adaptor Proteins, Signal Transducing - genetics
AKT1 protein
Autophagy
Autophagy - genetics
Breast cancer
Cancer
Carrier Proteins - biosynthesis
Carrier Proteins - genetics
Gene Expression Regulation, Neoplastic
HCT116 Cells
Humanities and Social Sciences
Humans
Kidney cancer
Kinases
Mechanistic Target of Rapamycin Complex 1
Membrane Proteins - biosynthesis
Membrane Proteins - genetics
multidisciplinary
Multiprotein Complexes - antagonists & inhibitors
Multiprotein Complexes - genetics
Neoplasms - genetics
Neoplasms - pathology
Nutrients
Phagocytosis
Phosphorylation
Proteomes
Proto-Oncogene Proteins c-akt - genetics
Pyruvate kinase
Pyruvic acid
Rapamycin
Renal cell carcinoma
Science
Science (multidisciplinary)
Signal Transduction - genetics
Thyroid Hormone-Binding Proteins
Thyroid Hormones - biosynthesis
Thyroid Hormones - genetics
TOR protein
TOR Serine-Threonine Kinases - antagonists & inhibitors
TOR Serine-Threonine Kinases - genetics
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Abstract 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.
AbstractList 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.
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.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.
ArticleNumber 21524
Author Zou, Han-Fa
Ye, Ming-Liang
Liu, Ze-Xian
Zhao, Jian-Yuan
Yao, Cui-Fang
He, Chang-Liang
Xu, Wei
Bian, Yang-Yang
Xue, Yu
Luo, Fang-Xiu
Zhao, Shi-Min
Zhou, Kai-Qiang
Lin, Yan
Qu, Yuan-Yuan
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  organization: Chinese Academy of Sciences, Dalian Institute Chemical Physics, National Chromatography R&A Center, Key Lab Separation Science Analytic Chemistry
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  organization: Department of Medical Engineering, College of Life Sciences and Technology, Huazhong University of Science and Technology
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  surname: Lin
  fullname: Lin, Yan
  organization: State Key Lab of Genetic Engineering, Obstetrics & Gynecology Hospital of Fudan University and School of Life Sciences, Shanghai 200090, P.R. China , Institutes of Biomedical Sciences and Collaborative Innovation Center for Genetics and Development Biology, Fudan University
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  surname: Luo
  fullname: Luo, Fang-Xiu
  organization: Department of Pathology, Affiliated Ruijin Hospital of Shanghai Jiaotong University
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  givenname: Yuan-Yuan
  surname: Qu
  fullname: Qu, Yuan-Yuan
  organization: Department of Urology, Fudan University Shanghai Cancer Center, Shanghai 200032, P.R. China, Department of Oncology, Shanghai Medical College, Fudan University
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  surname: Zhao
  fullname: Zhao, Jian-Yuan
  organization: State Key Lab of Genetic Engineering, Obstetrics & Gynecology Hospital of Fudan University and School of Life Sciences, Shanghai 200090, P.R. China , Collaborative Innovation Center for Biotherapy, West China Hospital, Sichuan University
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  surname: Zhao
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  email: zhaosm@fudan.edu.cn
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  surname: Xu
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  email: xuwei_0706@fudan.edu.cn
  organization: State Key Lab of Genetic Engineering, Obstetrics & Gynecology Hospital of Fudan University and School of Life Sciences, Shanghai 200090, P.R. China , Institutes of Biomedical Sciences and Collaborative Innovation Center for Genetics and Development Biology, Fudan University, Collaborative Innovation Center for Biotherapy, West China Hospital, Sichuan University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/26876154$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright The Author(s) 2016
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Snippet In cancer cells, the mammalian target of rapamycin complex 1 (mTORC1) that requires hormonal and nutrient signals for its activation, is constitutively...
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SubjectTerms 13
13/109
13/51
14
14-3-3 protein
14/63
38
38/1
38/70
38/77
631/67/2327
631/80/86
82
82/58
82/80
82/83
Adaptor Proteins, Signal Transducing - biosynthesis
Adaptor Proteins, Signal Transducing - genetics
AKT1 protein
Autophagy
Autophagy - genetics
Breast cancer
Cancer
Carrier Proteins - biosynthesis
Carrier Proteins - genetics
Gene Expression Regulation, Neoplastic
HCT116 Cells
Humanities and Social Sciences
Humans
Kidney cancer
Kinases
Mechanistic Target of Rapamycin Complex 1
Membrane Proteins - biosynthesis
Membrane Proteins - genetics
multidisciplinary
Multiprotein Complexes - antagonists & inhibitors
Multiprotein Complexes - genetics
Neoplasms - genetics
Neoplasms - pathology
Nutrients
Phagocytosis
Phosphorylation
Proteomes
Proto-Oncogene Proteins c-akt - genetics
Pyruvate kinase
Pyruvic acid
Rapamycin
Renal cell carcinoma
Science
Science (multidisciplinary)
Signal Transduction - genetics
Thyroid Hormone-Binding Proteins
Thyroid Hormones - biosynthesis
Thyroid Hormones - genetics
TOR protein
TOR Serine-Threonine Kinases - antagonists & inhibitors
TOR Serine-Threonine Kinases - genetics
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Title Pyruvate Kinase M2 Activates mTORC1 by Phosphorylating AKT1S1
URI https://link.springer.com/article/10.1038/srep21524
https://www.ncbi.nlm.nih.gov/pubmed/26876154
https://www.proquest.com/docview/1899020574
https://www.proquest.com/docview/1765921666
https://pubmed.ncbi.nlm.nih.gov/PMC4753445
Volume 6
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